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. 2014 Nov 17;10(1):28–51. doi: 10.1007/s11515-014-1338-7

Transcriptional regulation of secretory capacity by bZip transcription factors

Rebecca M Fox 1, Deborah J Andrew 1,✉
PMCID: PMC4374484  NIHMSID: NIHMS661189  PMID: 25821458

Abstract

Cells of specialized secretory organs expand their secretory pathways to accommodate the increased protein load necessary for their function. The endoplasmic reticulum (ER), the Golgi apparatus and the secretory vesicles, expand not only the membrane components but also the protein machinery required for increased protein production and transport. Increased protein load causes an ER stress response akin to the Unfolded Protein Response (UPR). Recent work has implicated several bZip transcription factors in the regulation of protein components of the early secretory pathway necessary to alleviate this stress. Here, we highlight eight bZip transcription factors in regulating secretory pathway component genes. These include components of the three canonical branches of the UPR-ATF4, XBP1, and ATF6, as well as the five members of the Creb3 family of transcription factors.We review findings from both invertebrate and vertebrate model systems suggesting that all of these proteins increase secretory capacity in response to increased protein load. Finally, we propose that the Creb3 family of factors may have a dual role in secretory cell differentiation by also regulating the pathways necessary for cell cycle exit during terminal differentiation.

Electronic Supplementary Material

Supplementary material is available for this article at 10.1007/s11515-014-1338-7 and is accessible for authorized users.

Keywords: bZip transcription factors, endoplasmic reticulum, Golgi, secretion, secretory capacity, secretory vesicles

Electronic supplementary material

11515_2014_1338_MOESM1_ESM.pdf (361.4KB, pdf)

Supplementary material, approximately 357 KB.

References

  1. Abrams E W, Andrew D J. Prolyl 4-hydroxylase alpha-related proteins in Drosophila melanogaster: tissue-specific embryonic expression of the 99F8-9 cluster. Mech Dev. 2002;112(1–2):165–171. doi: 10.1016/s0925-4773(01)00636-0. [DOI] [PubMed] [Google Scholar]
  2. Abrams E W, Andrew D J. CrebA regulates secretory activity in the Drosophila salivary gland and epidermis. Development. 2005;132(12):2743–2758. doi: 10.1242/dev.01863. [DOI] [PubMed] [Google Scholar]
  3. Adachi Y, Yamamoto K, Okada T, Yoshida H, Harada A, Mori K. ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum. Cell Struct Funct. 2008;33(1):75–89. doi: 10.1247/csf.07044. [DOI] [PubMed] [Google Scholar]
  4. Adham I M, Eck T J, Mierau K, Müller N, Sallam M A, Paprotta I, Schubert S, Hoyer-Fender S, Engel W. Reduction of spermatogenesis but not fertility in Creb3l4-deficient mice. Mol Cell Biol. 2005;25(17):7657–7664. doi: 10.1128/MCB.25.17.7657-7664.2005. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Aebi M. N-linked protein glycosylation in the ER. Biochim Biophys Acta. 2013;1833(11):2430–2437. doi: 10.1016/j.bbamcr.2013.04.001. [DOI] [PubMed] [Google Scholar]
  6. Alconada A, Bauer U, Hoflack B. A tyrosine-based motif and a casein kinase II phosphorylation site regulate the intracellular trafficking of the varicella-zoster virus glycoprotein I, a protein localized in the trans-Golgi network. EMBO J. 1996;15(22):6096–6110. [PMC free article] [PubMed] [Google Scholar]
  7. Antonin W, Meyer H A, Hartmann E. Interactions between Spc2p and other components of the endoplasmic reticulum translocation sites of the yeast Saccharomyces cerevisiae. J Biol Chem. 2000;275(44):34068–34072. doi: 10.1074/jbc.M006126200. [DOI] [PubMed] [Google Scholar]
  8. Appenzeller-Herzog C, Hauri H P. The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J Cell Sci. 2006;119(Pt11):2173–2183. doi: 10.1242/jcs.03019. [DOI] [PubMed] [Google Scholar]
  9. Aragón T, van Anken E, Pincus D, Serafimova I M, Korennykh A V, Rubio C A, Walter P. Messenger RNA targeting to endoplasmic reticulum stress signalling sites. Nature. 2009;457(7230):736–740. doi: 10.1038/nature07641. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Asada R, Kanemoto S, Kondo S, Saito A, Imaizumi K. The signalling from endoplasmic reticulum-resident bZIP transcription factors involved in diverse cellular physiology. J Biochem. 2011;149(5):507–518. doi: 10.1093/jb/mvr041. [DOI] [PubMed] [Google Scholar]
  11. Asada R, Saito A, Kawasaki N, Kanemoto S, Iwamoto H, Oki M, Miyagi H, Izumi S, Imaizumi K. The endoplasmic reticulum stress transducer OASIS is involved in the terminal differentiation of goblet cells in the large intestine. J Biol Chem. 2012;287(11):8144–8153. doi: 10.1074/jbc.M111.332593. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Ast T, Cohen G, Schuldiner M. A network of cytosolic factors targets SRP-independent proteins to the endoplasmic reticulum. Cell. 2013;152(5):1134–1145. doi: 10.1016/j.cell.2013.02.003. [DOI] [PubMed] [Google Scholar]
  13. Ast T, Schuldiner M. All roads lead to Rome (but some may be harder to travel): SRP-independent translocation into the endoplasmic reticulum. Crit Rev Biochem Mol Biol. 2013;48(3):273–288. doi: 10.3109/10409238.2013.782999. [DOI] [PubMed] [Google Scholar]
  14. Audas T E, Li Y, Liang G, Lu R. A novel protein, Luman/CREB3 recruitment factor, inhibits Luman activation of the unfolded protein response. Mol Cell Biol. 2008;28(12):3952–3966. doi: 10.1128/MCB.01439-07. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Bailey D, Barreca C, O’Hare P. Trafficking of the bZIP transmembrane transcription factor CREB-H into alternate pathways of ERAD and stress-regulated intramembrane proteolysis. Traffic. 2007;8(12):1796–1814. doi: 10.1111/j.1600-0854.2007.00654.x. [DOI] [PubMed] [Google Scholar]
  16. Bailey D, O’Hare P. Transmembrane bZIP transcription factors in ER stress signaling and the unfolded protein response. Antioxid Redox Signal. 2007;9(12):2305–2321. doi: 10.1089/ars.2007.1796. [DOI] [PubMed] [Google Scholar]
  17. Barbosa S, Fasanella G, Carreira S, Llarena M, Fox R, Barreca C, Andrew D, O’Hare P. An orchestrated program regulating secretory pathway genes and cargos by the transmembrane transcription factor CREB-H. Traffic. 2013;14(4):382–398. doi: 10.1111/tra.12038. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Barlowe C K, Miller E A. Secretory protein biogenesis and traffic in the early secretory pathway. Genetics. 2013;193(2):383–410. doi: 10.1534/genetics.112.142810. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Belmont P J, Chen WJ, San Pedro MN, Thuerauf D J, Gellings Lowe N, Gude N, Hilton B, Wolkowicz R, Sussman M A, Glembotski C C. Roles for endoplasmic reticulum-associated degradation and the novel endoplasmic reticulum stress response gene Derlin-3 in the ischemic heart. Circ Res. 2010;106(2):307–316. doi: 10.1161/CIRCRESAHA.109.203901. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Ben Aicha S, Lessard J, Pelletier M, Fournier A, Calvo E, Labrie C. Transcriptional profiling of genes that are regulated by the endoplasmic reticulum-bound transcription factor AIbZIP/CREB3L4 in prostate cells. Physiol Genomics. 2007;31(2):295–305. doi: 10.1152/physiolgenomics.00097.2007. [DOI] [PubMed] [Google Scholar]
  21. Berg R A, Prockop D J. The thermal transition of a nonhydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen. Biochem Biophys Res Commun. 1973;52(1):115–120. doi: 10.1016/0006-291x(73)90961-3. [DOI] [PubMed] [Google Scholar]
  22. Beznoussenko G V, Parashuraman S, Rizzo R, Polishchuk R, Martella O, Di Giandomenico D, Fusella A, Spaar A, Sallese M, Capestrano M G, Pavelka M, Vos M R, Rikers Y G, Helms V, Mironov A A, Luini A. Elife. 2014. Transport of soluble proteins through the Golgi occurs by diffusion via continuities across cisternae; p. 3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Bommiasamy H, Back S H, Fagone P, Lee K, Meshinchi S, Vink E, Sriburi R, Frank M, Jackowski S, Kaufman R J, Brewer J W. ATF6alpha induces XBP1-independent expansion of the endoplasmic reticulum. J Cell Sci. 2009;122(Pt10):1626–1636. doi: 10.1242/jcs.045625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Bonfanti L, Mironov A A, Jr, Martínez-Menárguez J A, Martella O, Fusella A, Baldassarre M, Buccione R, Geuze H J, Mironov A A, Jr, Luini A. Procollagen traverses the Golgi stack without leaving the lumen of cisternae: evidence for cisternal maturation. Cell. 1998;95(7):993–1003. doi: 10.1016/s0092-8674(00)81723-7. [DOI] [PubMed] [Google Scholar]
  25. Borgese N, Fasana E. Targeting pathways of C-tail-anchored proteins. Biochim Biophys Acta. 2011;1808(3):937–946. doi: 10.1016/j.bbamem.2010.07.010. [DOI] [PubMed] [Google Scholar]
  26. Braakman I, Bulleid N J. Protein folding and modification in the mammalian endoplasmic reticulum. Annu Rev Biochem. 2011;80(1):71–99. doi: 10.1146/annurev-biochem-062209-093836. [DOI] [PubMed] [Google Scholar]
  27. Brandizzi F, Barlowe C. Organization of the ER-Golgi interface for membrane traffic control. Nat Rev Mol Cell Biol. 2013;14(6):382–392. doi: 10.1038/nrm3588. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Bridgewater L C, Lefebvre V, de Crombrugghe B. Chondrocytespecific enhancer elements in the Col11a2 gene resemble the Col2a1 tissue-specific enhancer. J Biol Chem. 1998;273(24):14998–15006. doi: 10.1074/jbc.273.24.14998. [DOI] [PubMed] [Google Scholar]
  29. Bulleid N J. Disulfide bond formation in the mammalian endoplasmic reticulum. Cold Spring Harb Perspect Biol. 2012;4(11):4. doi: 10.1101/cshperspect.a013219. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Bulleid N J, Ellgaard L. Multiple ways to make disulfides. Trends Biochem Sci. 2011;36(9):485–492. doi: 10.1016/j.tibs.2011.05.004. [DOI] [PubMed] [Google Scholar]
  31. Calfon M, Zeng H, Urano F, Till J H, Hubbard S R, Harding H P, Clark S G, Ron D. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature. 2002;415(6867):92–96. doi: 10.1038/415092a. [DOI] [PubMed] [Google Scholar]
  32. Capitani M, Sallese M. The KDEL receptor: new functions for an old protein. FEBS Lett. 2009;583(23):3863–3871. doi: 10.1016/j.febslet.2009.10.053. [DOI] [PubMed] [Google Scholar]
  33. Capoccia B J, Jin R U, Kong Y Y, Peek R M, Jr, Fassan M, Rugge M, Mills J C. The ubiquitin ligase Mindbomb 1 coordinates gastrointestinal secretory cell maturation. J Clin Invest. 2013;123(4):1475–1491. doi: 10.1172/JCI65703. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Carlton J, Bujny M, Peter B J, Oorschot V M, Rutherford A, Mellor H, Klumperman J, McMahon H T, Cullen P J. Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high-curvature membranes and 3-phosphoinositides. Curr Biol. 2004;14(20):1791–1800. doi: 10.1016/j.cub.2004.09.077. [DOI] [PubMed] [Google Scholar]
  35. Carrasco D R, Sukhdeo K, Protopopova M, Sinha R, Enos M, Carrasco D E, Zheng M, Mani M, Henderson J, Pinkus G S, Munshi N, Horner J, Ivanova E V, Protopopov A, Anderson K C, Tonon G, DePinho R A. The differentiation and stress response factor XBP-1 drives multiple myeloma pathogenesis. Cancer Cell. 2007;11(4):349–360. doi: 10.1016/j.ccr.2007.02.015. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Chan C P, Mak T Y, Chin K T, Ng I O, Jin D Y. N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H. J Cell Sci. 2010;123(Pt9):1438–1448. doi: 10.1242/jcs.067819. [DOI] [PubMed] [Google Scholar]
  37. Chapuy B, Tikkanen R, Mühlhausen C, Wenzel D, von Figura K, Höning S. AP-1 and AP-3 mediate sorting of melanosomal and lysosomal membrane proteins into distinct post-Golgi trafficking pathways. Traffic. 2008;9(7):1157–1172. doi: 10.1111/j.1600-0854.2008.00745.x. [DOI] [PubMed] [Google Scholar]
  38. Chartron J W, Gonzalez G M, Clemons W M., Jr A structural model of the Sgt2 protein and its interactions with chaperones and the Get4/Get5 complex. J Biol Chem. 2011;286(39):34325–34334. doi: 10.1074/jbc.M111.277798. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Chen S, Novick P, Ferro-Novick S. ER structure and function. Curr Opin Cell Biol. 2013;25(4):428–433. doi: 10.1016/j.ceb.2013.02.006. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Chin K T, Zhou H J, Wong C M, Lee J M, Chan C P, Qiang B Q, Yuan J G, Ng I O, Jin D Y. The liver-enriched transcription factor CREB-H is a growth suppressor protein underexpressed in hepatocellular carcinoma. Nucleic Acids Res. 2005;33(6):1859–1873. doi: 10.1093/nar/gki332. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Cobbold C, Coventry J, Ponnambalam S, Monaco A P. Actin and microtubule regulation of trans-Golgi network architecture, and copper-dependent protein transport to the cell surface. Mol Membr Biol. 2004;21(1):59–66. doi: 10.1080/096870310001607350. [DOI] [PubMed] [Google Scholar]
  42. Cosson P, Lefkir Y, Démollière C, Letourneur F. New COP1-binding motifs involved in ER retrieval. EMBO J. 1998;17(23):6863–6870. doi: 10.1093/emboj/17.23.6863. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Cosson P, Schröder-Köhne S, Sweet D S, Démollière C, Hennecke S, Frigerio G, Letourneur F. The Sec20/Tip20p complex is involved in ER retrieval of dilysine-tagged proteins. Eur J Cell Biol. 1997;73(2):93–97. [PubMed] [Google Scholar]
  44. Cottam N P, Ungar D. Retrograde vesicle transport in the Golgi. Protoplasma. 2012;249(4):943–955. doi: 10.1007/s00709-011-0361-7. [DOI] [PubMed] [Google Scholar]
  45. Cox J S, Walter P. A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell. 1996;87(3):391–404. doi: 10.1016/s0092-8674(00)81360-4. [DOI] [PubMed] [Google Scholar]
  46. Cross B C, Bond P J, Sadowski P G, Jha B K, Zak J, Goodman J M, Silverman R H, Neubert T A, Baxendale I R, Ron D, Harding H P. The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule. Proc Natl Acad Sci USA. 2012;109(15):E869–E878. doi: 10.1073/pnas.1115623109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Cross B C, Sinning I, Luirink J, High S. Delivering proteins for export from the cytosol. Nat Rev Mol Cell Biol. 2009;10(4):255–264. doi: 10.1038/nrm2657. [DOI] [PubMed] [Google Scholar]
  48. Csala M, Kereszturi, Mandl J, Bánhegyi G. The endoplasmic reticulum as the extracellular space inside the cell: role in protein folding and glycosylation. Antioxid Redox Signal. 2012;16(10):1100–1108. doi: 10.1089/ars.2011.4227. [DOI] [PubMed] [Google Scholar]
  49. Cui-Wang T, Hanus C, Cui T, Helton T, Bourne J, Watson D, Harris K M, Ehlers M D. Local zones of endoplasmic reticulum complexity confine cargo in neuronal dendrites. Cell. 2012;148(1–2):309–321. doi: 10.1016/j.cell.2011.11.056. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. D’Alessio C, Caramelo J J, Parodi A J. UDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control. Semin Cell Dev Biol. 2010;21(5):491–499. doi: 10.1016/j.semcdb.2009.12.014. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. D’Arcangelo J G, Stahmer K R, Miller E A. Vesicle-mediated export from the ER: COPII coat function and regulation. Biochim Biophys Acta. 2013;1833(11):2464–2472. doi: 10.1016/j.bbamcr.2013.02.003. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Dancourt J, Barlowe C. Protein sorting receptors in the early secretory pathway. Annu Rev Biochem. 2010;79(1):777–802. doi: 10.1146/annurev-biochem-061608-091319. [DOI] [PubMed] [Google Scholar]
  53. Delic M, Rebnegger C, Wanka F, Puxbaum V, Haberhauer-Troyer C, Hann S, Köllensperger G, Mattanovich D, Gasser B. Oxidative protein folding and unfolded protein response elicit differing redox regulation in endoplasmic reticulum and cytosol of yeast. Free Radic Biol Med. 2012;52(9):2000–2012. doi: 10.1016/j.freeradbiomed.2012.02.048. [DOI] [PubMed] [Google Scholar]
  54. Delic M, Valli M, Graf A B, Pfeffer M, Mattanovich D, Gasser B. The secretory pathway: exploring yeast diversity. FEMS Microbiol Rev. 2013;37(6):872–914. doi: 10.1111/1574-6976.12020. [DOI] [PubMed] [Google Scholar]
  55. Denard B, CLee, Ye J. Doxorubicin blocks proliferation of cancer cells through proteolytic activation of CREB3L1. eLife. 2012;1:e00090. doi: 10.7554/eLife.00090. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Denard B, Seemann J, Chen Q, Gay A, Huang H, Chen Y, Ye J. The membrane-bound transcription factor CREB3L1 is activated in response to virus infection to inhibit proliferation of virus-infected cells. Cell Host Microbe. 2011;10(1):65–74. doi: 10.1016/j.chom.2011.06.006. [DOI] [PMC free article] [PubMed] [Google Scholar]
  57. Denic V. A portrait of the GET pathway as a surprisingly complicated young man. Trends Biochem Sci. 2012;37(10):411–417. doi: 10.1016/j.tibs.2012.07.004. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Denic V, Dötsch V, Sinning I. Endoplasmic reticulum targeting and insertion of tail-anchored membrane proteins by the GET pathway. Cold Spring Harb Perspect Biol. 2013;5(8):a013334. doi: 10.1101/cshperspect.a013334. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Deprez P, Gautschi M, Helenius A. More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle. Mol Cell. 2005;19(2):183–195. doi: 10.1016/j.molcel.2005.05.029. [DOI] [PubMed] [Google Scholar]
  60. Egea P F, Stroud R M, Walter P. Targeting proteins to membranes: structure of the signal recognition particle. Curr Opin Struct Biol. 2005;15(2):213–220. doi: 10.1016/j.sbi.2005.03.007. [DOI] [PubMed] [Google Scholar]
  61. Eleveld-Trancikova D, Sanecka A, van Hout-Kuijer MA, Looman MW, Hendriks I A, Jansen B J, Adema G J. DC-STAMP interacts with ER-resident transcription factor LUMAN which becomes activated during DC maturation. Mol Immunol. 2010;47(11–12):1963–1973. doi: 10.1016/j.molimm.2010.04.019. [DOI] [PubMed] [Google Scholar]
  62. Ellgaard L, Helenius A. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol. 2003;4(3):181–191. doi: 10.1038/nrm1052. [DOI] [PubMed] [Google Scholar]
  63. Fang H, Mullins C, Green N. In addition to SEC11, a newly identified gene, SPC3, is essential for signal peptidase activity in the yeast endoplasmic reticulum. J Biol Chem. 1997;272(20):13152–13158. doi: 10.1074/jbc.272.20.13152. [DOI] [PubMed] [Google Scholar]
  64. Fang H, Panzner S, Mullins C, Hartmann E, Green N. The homologue of mammalian SPC12 is important for efficient signal peptidase activity in Saccharomyces cerevisiae. J Biol Chem. 1996;271(28):16460–16465. doi: 10.1074/jbc.271.28.16460. [DOI] [PubMed] [Google Scholar]
  65. Feldheim D, Schekman R. Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex. J Cell Biol. 1994;126(4):935–943. doi: 10.1083/jcb.126.4.935. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Fölsch H, Pypaert M, Schu P, Mellman I. Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells. J Cell Biol. 2001;152(3):595–606. doi: 10.1083/jcb.152.3.595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Fox R M, Hanlon C D, Andrew D J. The CrebA/Creb3-like transcription factors are major and direct regulators of secretory capacity. J Cell Biol. 2010;191(3):479–492. doi: 10.1083/jcb.201004062. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Fox R M, Vaishnavi A, Maruyama R, Andrew D J. Organspecific gene expression: the bHLH protein Sage provides tissue specificity to Drosophila FoxA. Development. 2013;140(10):2160–2171. doi: 10.1242/dev.092924. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. Frand A R, Cuozzo J W, Kaiser C A. Pathways for protein disulphide bond formation. Trends Cell Biol. 2000;10(5):203–210. doi: 10.1016/s0962-8924(00)01745-1. [DOI] [PubMed] [Google Scholar]
  70. Friedlander M, Blobel G. Bovine opsin has more than one signal sequence. Nature. 1985;318(6044):338–343. doi: 10.1038/318338a0. [DOI] [PubMed] [Google Scholar]
  71. Fujimoto Y, Watanabe Y, Uchida M, Ozaki M. Mammalian signal peptidase: partial purification and general characterization of the signal peptidase from microsomal membranes of porcine pancreas. J Biochem. 1984;96(4):1125–1131. doi: 10.1093/oxfordjournals.jbchem.a134930. [DOI] [PubMed] [Google Scholar]
  72. Funamoto T, Sekimoto T, Murakami T, Kurogi S, Imaizumi K, Chosa E. Roles of the endoplasmic reticulum stress transducer OASIS in fracture healing. Bone. 2011;49(4):724–732. doi: 10.1016/j.bone.2011.06.012. [DOI] [PubMed] [Google Scholar]
  73. Gardner B M, Pincus D, Gotthardt K, Gallagher C M, Walter P. Endoplasmic reticulum stress sensing in the unfolded protein response. Cold Spring Harb Perspect Biol. 2013;5(3):a013169. doi: 10.1101/cshperspect.a013169. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Gaynor E C, te Heesen S, Graham T R, Aebi M, Emr S D. Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast. J Cell Biol. 1994;127(3):653–665. doi: 10.1083/jcb.127.3.653. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Gidalevitz T, Stevens F, Argon Y. Orchestration of secretory protein folding by ER chaperones. Biochim Biophys Acta. 2013;1833(11):2410–2424. doi: 10.1016/j.bbamcr.2013.03.007. [DOI] [PMC free article] [PubMed] [Google Scholar]
  76. Gillon A D, Latham C F, Miller E A. Vesicle-mediated ER export of proteins and lipids. Biochim Biophys Acta. 2012;1821(8):1040–1049. doi: 10.1016/j.bbalip.2012.01.005. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. Gilmore R, Blobel G. Transient involvement of signal recognition particle and its receptor in the microsomal membrane prior to protein translocation. Cell. 1983;35(3Pt2):677–685. doi: 10.1016/0092-8674(83)90100-9. [DOI] [PubMed] [Google Scholar]
  78. Gilmore R, Blobel G, Walter P. Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle. J Cell Biol. 1982;95(2Pt1):463–469. doi: 10.1083/jcb.95.2.463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Gleeson P A, Lock J G, Luke M R, Stow J L. Domains of the TGN: coats, tethers and G proteins. Traffic. 2004;5(5):315–326. doi: 10.1111/j.1398-9219.2004.00182.x. [DOI] [PubMed] [Google Scholar]
  80. Glick B S, Luini A. Models for Golgi traffic: a critical assessment. Cold Spring Harb Perspect Biol. 2011;3(11):a005215. doi: 10.1101/cshperspect.a005215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  81. Gorres K L, Raines R T. Prolyl 4-hydroxylase. Crit Rev Biochem Mol Biol. 2010;45(2):106–124. doi: 10.3109/10409231003627991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  82. Greenburg G, Shelness G S, Blobel G. A subunit of mammalian signal peptidase is homologous to yeast SEC11 protein. J Biol Chem. 1989;264(27):15762–15765. [PubMed] [Google Scholar]
  83. Gregorieff A, Stange D E, Kujala P, Begthel H, van den Born M, Korving J, Peters P J, Clevers H. The ets-domain transcription factor Spdef promotes maturation of goblet and paneth cells in the intestinal epithelium. Gastroenterology. 2009;137:1333–1345. doi: 10.1053/j.gastro.2009.06.044. [DOI] [PubMed] [Google Scholar]
  84. Gristick H B, Rao M, Chartron J W, Rome M E, Shan S O, Clemons W M., Jr Crystal structure of ATP-bound Get3-Get4-Get5 complex reveals regulation of Get3 by Get4. Nat Struct Mol Biol. 2014;21(5):437–442. doi: 10.1038/nsmb.2813. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Grueber W B, Jan L Y, Jan Y N. Different levels of the homeodomain protein cut regulate distinct dendrite branching patterns of Drosophila multidendritic neurons. Cell. 2003;112(6):805–818. doi: 10.1016/s0092-8674(03)00160-0. [DOI] [PubMed] [Google Scholar]
  86. Guo X, Mattera R, Ren X, Chen Y, Retamal C, González A, Bonifacino J S. The adaptor protein-1 μ1B subunit expands the repertoire of basolateral sorting signal recognition in epithelial cells. Dev Cell. 2013;27(3):353–366. doi: 10.1016/j.devcel.2013.10.006. [DOI] [PMC free article] [PubMed] [Google Scholar]
  87. Guo Y, Zanetti G, Schekman R. A novel GTP-binding proteinadaptor protein complex responsible for export of Vangl2 from the trans Golgi network. Elife. 2013;2:e00160. doi: 10.7554/eLife.00160. [DOI] [PMC free article] [PubMed] [Google Scholar]
  88. Guzman N A, Rojas F J, Cutroneo K R. Collagen lysyl hydroxylation occurs within the cisternae of the rough endoplasmic reticulum. Arch Biochem Biophys. 1976;172(2):449–454. doi: 10.1016/0003-9861(76)90097-7. [DOI] [PubMed] [Google Scholar]
  89. Hamman B D, Hendershot L M, Johnson A E. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell. 1998;92(6):747–758. doi: 10.1016/s0092-8674(00)81403-8. [DOI] [PubMed] [Google Scholar]
  90. Han J, Back S H, Hur J, Lin Y H, Gildersleeve R, Shan J, Yuan C L, Krokowski D, Wang S, Hatzoglou M, Kilberg M S, Sartor M A, Kaufman R J. ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death. Nat Cell Biol. 2013;15(5):481–490. doi: 10.1038/ncb2738. [DOI] [PMC free article] [PubMed] [Google Scholar]
  91. Harding H P, Novoa I, Zhang Y, Zeng H, Wek R, Schapira M, Ron D. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell. 2000;6(5):1099–1108. doi: 10.1016/s1097-2765(00)00108-8. [DOI] [PubMed] [Google Scholar]
  92. Harding H P, Zhang Y, Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature. 1999;397(6716):271–274. doi: 10.1038/16729. [DOI] [PubMed] [Google Scholar]
  93. Harding H P, Zhang Y, Zeng H, Novoa I, Lu P D, Calfon M, Sadri N, Yun C, Popko B, Paules R, Stojdl D F, Bell J C, Hettmann T, Leiden J M, Ron D. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell. 2003;11(3):619–633. doi: 10.1016/s1097-2765(03)00105-9. [DOI] [PubMed] [Google Scholar]
  94. Haze K, Okada T, Yoshida H, Yanagi H, Yura T, Negishi M, Mori K. Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to activating transcription factor 6 as a transcriptional activator of the mammalian unfolded protein response. Biochem J. 2001;355(Pt1):19–28. doi: 10.1042/0264-6021:3550019. [DOI] [PMC free article] [PubMed] [Google Scholar]
  95. Haze K, Yoshida H, Yanagi H, Yura T, Mori K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell. 1999;10(11):3787–3799. doi: 10.1091/mbc.10.11.3787. [DOI] [PMC free article] [PubMed] [Google Scholar]
  96. Heuer D, Rejman Lipinski A, Machuy N, Karlas A, Wehrens A, Siedler F, Brinkmann V, Meyer T F. Chlamydia causes fragmentation of the Golgi compartment to ensure reproduction. Nature. 2009;457(7230):731–735. doi: 10.1038/nature07578. [DOI] [PubMed] [Google Scholar]
  97. Hino K, Saito A, Kido M, Kanemoto S, Asada R, Takai T, Cui M, Cui X, Imaizumi K. J Biol Chem. 2014. Master regulator for chondrogenesis, Sox9, regulates transcriptional activation of the ER stress transducer BBF2H7/CREB3L2 in chondrocytes. [DOI] [PMC free article] [PubMed] [Google Scholar]
  98. Hirschberg C B, Robbins P W, Abeijon C. Transporters of nucleotide sugars, ATP, and nucleotide sulfate in the endoplasmic reticulum and Golgi apparatus. Annu Rev Biochem. 1998;67(1):49–69. doi: 10.1146/annurev.biochem.67.1.49. [DOI] [PubMed] [Google Scholar]
  99. Hirst J, Irving C, Borner G H. Adaptor protein complexes AP-4 and AP-5: new players in endosomal trafficking and progressive spastic paraplegia. Traffic. 2013;14(2):153–164. doi: 10.1111/tra.12028. [DOI] [PubMed] [Google Scholar]
  100. Hollien J, Lin J H, Li H, Stevens N, Walter P, Weissman J S. Regulated Ire1-dependent decay of messenger RNAs in mammalian cells. J Cell Biol. 2009;186(3):323–331. doi: 10.1083/jcb.200903014. [DOI] [PMC free article] [PubMed] [Google Scholar]
  101. Hollien J, Weissman J S. Decay of endoplasmic reticulumlocalized mRNAs during the unfolded protein response. Science. 2006;313(5783):104–107. doi: 10.1126/science.1129631. [DOI] [PubMed] [Google Scholar]
  102. Hu C C, Dougan S K, McGehee A M, Love J C, Ploegh H L. XBP-1 regulates signal transduction, transcription factors and bone marrow colonization in B cells. EMBO J. 2009;28(11):1624–1636. doi: 10.1038/emboj.2009.117. [DOI] [PMC free article] [PubMed] [Google Scholar]
  103. Huh W J, Esen E, Geahlen J H, Bredemeyer A J, Lee A H, Shi G, Konieczny S F, Glimcher L H, Mills J C. XBP1 controls maturation of gastric zymogenic cells by induction of MIST1 and expansion of the rough endoplasmic reticulum. Gastroenterology. 2010;139(6):2038–2049. doi: 10.1053/j.gastro.2010.08.050. [DOI] [PMC free article] [PubMed] [Google Scholar]
  104. Hulmes D J S. Vertebrate Collagens-Structures, Functions and Biomedical Applications. In: Scheibel T, editor. Fibrous Proteins. Austin: Landes Bioscience; 2008. pp. 12–29. [Google Scholar]
  105. Iyer S C, Ramachandran Iyer E P, Meduri R, Rubaharan M, Kuntimaddi A, Karamsetty M, Cox D N. Cut, via CrebA, transcriptionally regulates the COPII secretory pathway to direct dendrite development in Drosophila. J Cell Sci. 2013;126(Pt20):4732–4745. doi: 10.1242/jcs.131144. [DOI] [PMC free article] [PubMed] [Google Scholar]
  106. Jacob R, Naim H Y. Apical membrane proteins are transported in distinct vesicular carriers. Curr Biol. 2001;11(18):1444–1450. doi: 10.1016/s0960-9822(01)00446-8. [DOI] [PubMed] [Google Scholar]
  107. Janda C Y, Li J, Oubridge C, Hernández H, Robinson C V, Nagai K. Recognition of a signal peptide by the signal recognition particle. Nature. 2010;465(7297):507–510. doi: 10.1038/nature08870. [DOI] [PMC free article] [PubMed] [Google Scholar]
  108. Jang S Y, Jang SW, Ko J. Regulation of ADP-ribosylation factor 4 expression by small leucine zipper protein and involvement in breast cancer cell migration. Cancer Lett. 2012;314(2):185–197. doi: 10.1016/j.canlet.2011.09.028. [DOI] [PubMed] [Google Scholar]
  109. Jiang Y, Cheng Z, Mandon E C, Gilmore R. An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation. J Cell Biol. 2008;180(6):1149–1161. doi: 10.1083/jcb.200707196. [DOI] [PMC free article] [PubMed] [Google Scholar]
  110. Jin D Y, Wang H L, Zhou Y, Chun A C, Kibler K V, Hou Y D, Kung H, Jeang K T. Hepatitis C virus core protein-induced loss of LZIP function correlates with cellular transformation. EMBO J. 2000;19(4):729–740. doi: 10.1093/emboj/19.4.729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  111. Johnson A E, van Waes MA. The translocon: a dynamic gateway at the ER membrane. Annu Rev Cell Dev Biol. 1999;15(1):799–842. doi: 10.1146/annurev.cellbio.15.1.799. [DOI] [PubMed] [Google Scholar]
  112. Johnson N, Powis K, High S. Post-translational translocation into the endoplasmic reticulum. Biochim Biophys Acta. 2013;1833(11):2403–2409. doi: 10.1016/j.bbamcr.2012.12.008. [DOI] [PubMed] [Google Scholar]
  113. Johnston H D, Foote C, Santeford A, Nothwehr S F. Golgi-to-late endosome trafficking of the yeast pheromone processing enzyme Ste13p is regulated by a phosphorylation site in its cytosolic domain. Mol Biol Cell. 2005;16(3):1456–1468. doi: 10.1091/mbc.E04-07-0642. [DOI] [PMC free article] [PubMed] [Google Scholar]
  114. Kalies K U, Hartmann E. Membrane topology of the 12- and the 25-kDa subunits of the mammalian signal peptidase complex. J Biol Chem. 1996;271(7):3925–3929. doi: 10.1074/jbc.271.7.3925. [DOI] [PubMed] [Google Scholar]
  115. Kaluza G, Repges S, McDowell W. The significance of carbohydrate trimming for the antigenicity of the Semliki Forest virus glycoprotein E2. Virology. 1990;176(2):369–378. doi: 10.1016/0042-6822(90)90007-e. [DOI] [PubMed] [Google Scholar]
  116. Kametaka S, Sawada N, Bonifacino J S, Waguri S. Functional characterization of protein-sorting machineries at the trans-Golgi network in Drosophila melanogaster. J Cell Sci. 2010;123(Pt3):460–471. doi: 10.1242/jcs.055103. [DOI] [PMC free article] [PubMed] [Google Scholar]
  117. Keenan R J, Freymann D M, Stroud R M, Walter P. The signal recognition particle. Annu Rev Biochem. 2001;70(1):755–775. doi: 10.1146/annurev.biochem.70.1.755. [DOI] [PubMed] [Google Scholar]
  118. Kienzle C, von Blume J. Secretory cargo sorting at the trans-Golgi network. Trends Cell Biol. 2014;24(10):584–593. doi: 10.1016/j.tcb.2014.04.007. [DOI] [PubMed] [Google Scholar]
  119. Kimata Y, Ishiwata-Kimata Y, Ito T, Hirata A, Suzuki T, Oikawa D, Takeuchi M, Kohno K. Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins. J Cell Biol. 2007;179(1):75–86. doi: 10.1083/jcb.200704166. [DOI] [PMC free article] [PubMed] [Google Scholar]
  120. Kivirikko K I, Myllyla R, Pihlajaniemi T. Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit. FASEB J. 1989;3:1609–1617. [PubMed] [Google Scholar]
  121. Ko J, Jang SW, Kim Y S, Kim I S, Sung H J, Kim H H, Park J Y, Lee Y H, Kim J, Na D S. Human LZIP binds to CCR1 and differentially affects the chemotactic activities of CCR1-dependent chemokines. FASEB J. 2004;18:890–892. doi: 10.1096/fj.03-0867fje. [DOI] [PubMed] [Google Scholar]
  122. Kode A, Mosialou I, Silva B C, Joshi S, Ferron M, Rached M T, Kousteni S. FoxO1 protein cooperates with ATF4 protein in osteoblasts to control glucose homeostasis. J Biol Chem. 2012;287(12):8757–8768. doi: 10.1074/jbc.M111.282897. [DOI] [PMC free article] [PubMed] [Google Scholar]
  123. Kondo S, Saito A, Hino S, Murakami T, Ogata M, Kanemoto S, Nara S, Yamashita A, Yoshinaga K, Hara H, Imaizumi K. BBF2H7, a novel transmembrane bZIP transcription factor, is a new type of endoplasmic reticulum stress transducer. Mol Cell Biol. 2007;27(5):1716–1729. doi: 10.1128/MCB.01552-06. [DOI] [PMC free article] [PubMed] [Google Scholar]
  124. Korennykh A V, Egea P F, Korostelev A A, Finer-Moore J, Zhang C, Shokat K M, Stroud R M, Walter P. The unfolded protein response signals through high-order assembly of Ire1. Nature. 2009;457(7230):687–693. doi: 10.1038/nature07661. [DOI] [PMC free article] [PubMed] [Google Scholar]
  125. Kutay U, Hartmann E, Rapoport T A. A class of membrane proteins with a C-terminal anchor. Trends Cell Biol. 1993;3(3):72–75. doi: 10.1016/0962-8924(93)90066-a. [DOI] [PubMed] [Google Scholar]
  126. Lavieu G, Zheng H, Rothman J E. Stapled Golgi cisternae remain in place as cargo passes through the stack. Elife. 2013;2:e00558. doi: 10.7554/eLife.00558. [DOI] [PMC free article] [PubMed] [Google Scholar]
  127. Lee A H, Heidtman K, Hotamisligil G S, Glimcher L H. Dual and opposing roles of the unfolded protein response regulated by IRE1alpha and XBP1 in proinsulin processing and insulin secretion. Proc Natl Acad Sci USA. 2011;108(21):8885–8890. doi: 10.1073/pnas.1105564108. [DOI] [PMC free article] [PubMed] [Google Scholar]
  128. Lee A H, Iwakoshi N N, Glimcher L H. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol. 2003;23(21):7448–7459. doi: 10.1128/MCB.23.21.7448-7459.2003. [DOI] [PMC free article] [PubMed] [Google Scholar]
  129. Lee J H, Giannikopoulos P, Duncan S A, Wang J, Johansen C T, Brown J D, Plutzky J, Hegele R A, Glimcher L H, Lee A H. The transcription factor cyclic AMP-responsive element-binding protein H regulates triglyceride metabolism. Nat Med. 2011;17(7):812–815. doi: 10.1038/nm.2347. [DOI] [PMC free article] [PubMed] [Google Scholar]
  130. Lee M W, Chanda D, Yang J, Oh H, Kim S S, Yoon Y S, Hong S, Park K G, Lee I K, Choi C S, Hanson R W, Choi H S, Koo S H. Regulation of hepatic gluconeogenesis by an ER-bound transcription factor, CREBH. Cell Metab. 2010;11(4):331–339. doi: 10.1016/j.cmet.2010.02.016. [DOI] [PubMed] [Google Scholar]
  131. Lefebvre V, Huang W, Harley V R, Goodfellow P N, de Crombrugghe B. SOX9 is a potent activator of the chondrocyte-specific enhancer of the pro alpha1(II) collagen gene. Mol Cell Biol. 1997;17(4):2336–2346. doi: 10.1128/mcb.17.4.2336. [DOI] [PMC free article] [PubMed] [Google Scholar]
  132. Liang G, Audas T E, Li Y, Cockram G P, Dean J D, Martyn A C, Kokame K, Lu R. Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element. Mol Cell Biol. 2006;26(21):7999–8010. doi: 10.1128/MCB.01046-06. [DOI] [PMC free article] [PubMed] [Google Scholar]
  133. Liang H, Van Valkenburgh C, Chen X, Mullins C, Van Kaer L, Green N, Fang H. Genetic complementation in yeast reveals functional similarities between the catalytic subunits of mammalian signal peptidase complex. J Biol Chem. 2003;278(51):50932–50939. doi: 10.1074/jbc.M307542200. [DOI] [PubMed] [Google Scholar]
  134. Losev E, Reinke C A, Jellen J, Strongin D E, Bevis B J, Glick B S. Golgi maturation visualized in living yeast. Nature. 2006;441(7096):1002–1006. doi: 10.1038/nature04717. [DOI] [PubMed] [Google Scholar]
  135. Lu R, Misra V. Potential role for luman, the cellular homologue of herpes simplex virus VP16 (alpha gene trans-inducing factor), in herpesvirus latency. J Virol. 2000;74(2):934–943. doi: 10.1128/jvi.74.2.934-943.2000. [DOI] [PMC free article] [PubMed] [Google Scholar]
  136. Lu R, Yang P, O’Hare P, Misra V. Luman, a new member of the CREB/ATF family, binds to herpes simplex virus VP16-associated host cellular factor. Mol Cell Biol. 1997;17(9):5117–5126. doi: 10.1128/mcb.17.9.5117. [DOI] [PMC free article] [PubMed] [Google Scholar]
  137. Luini A. A brief history of the cisternal progression-maturation model. Cell Logist. 2011;1(1):6–11. doi: 10.4161/cl.1.1.14693. [DOI] [PMC free article] [PubMed] [Google Scholar]
  138. Luo B, Lee A S. The critical roles of endoplasmic reticulum chaperones and unfolded protein response in tumorigenesis and anticancer therapies. Oncogene. 2013;32(7):805–818. doi: 10.1038/onc.2012.130. [DOI] [PMC free article] [PubMed] [Google Scholar]
  139. Määttänen P, Gehring K, Bergeron J J, Thomas D Y. Protein quality control in the ER: the recognition of misfolded proteins. Semin Cell Dev Biol. 2010;21(5):500–511. doi: 10.1016/j.semcdb.2010.03.006. [DOI] [PubMed] [Google Scholar]
  140. Mandon E C, Trueman S F, Gilmore R. Translocation of proteins through the Sec61 and SecYEG channels. Curr Opin Cell Biol. 2009;21(4):501–507. doi: 10.1016/j.ceb.2009.04.010. [DOI] [PMC free article] [PubMed] [Google Scholar]
  141. Mandon E C, Trueman S F, Gilmore R. Protein translocation across the rough endoplasmic reticulum. Cold Spring Harb Perspect Biol. 2013;5(2):5. doi: 10.1101/cshperspect.a013342. [DOI] [PMC free article] [PubMed] [Google Scholar]
  142. Mariappan M, Li X, Stefanovic S, Sharma A, Mateja A, Keenan R J, Hegde R S. A ribosome-associating factor chaperones tailanchored membrane proteins. Nature. 2010;466(7310):1120–1124. doi: 10.1038/nature09296. [DOI] [PMC free article] [PubMed] [Google Scholar]
  143. Martinez-Menárguez J A, Prekeris R, Oorschot V M, Scheller R, Slot J W, Geuze H J, Klumperman J. Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport. J Cell Biol. 2001;155(7):1213–1224. doi: 10.1083/jcb.200108029. [DOI] [PMC free article] [PubMed] [Google Scholar]
  144. Matlack K E, Misselwitz B, Plath K, Rapoport T A. BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell. 1999;97(5):553–564. doi: 10.1016/s0092-8674(00)80767-9. [DOI] [PubMed] [Google Scholar]
  145. Matsuura-Tokita K, Takeuchi M, Ichihara A, Mikuriya K, Nakano A. Live imaging of yeast Golgi cisternal maturation. Nature. 2006;441(7096):1007–1010. doi: 10.1038/nature04737. [DOI] [PubMed] [Google Scholar]
  146. McBride C E, Li J, Machamer C E. The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein. J Virol. 2007;81(5):2418–2428. doi: 10.1128/JVI.02146-06. [DOI] [PMC free article] [PubMed] [Google Scholar]
  147. McGehee A M, Dougan S K, Klemm E J, Shui G, Park B, Kim Y M, Watson N, Wenk M R, Ploegh H L, Hu C C. XBP-1-deficient plasmablasts show normal protein folding but altered glycosylation and lipid synthesis. J Immunol. 2009;183(6):3690–3699. doi: 10.4049/jimmunol.0900953. [DOI] [PMC free article] [PubMed] [Google Scholar]
  148. Mellor P, Deibert L, Calvert B, Bonham K, Carlsen S A, Anderson D H. CREB3L1 is a metastasis suppressor that represses expression of genes regulating metastasis, invasion, and angiogenesis. Mol Cell Biol. 2013;33(24):4985–4995. doi: 10.1128/MCB.00959-13. [DOI] [PMC free article] [PubMed] [Google Scholar]
  149. Melville D B, Montero-Balaguer M, Levic D S, Bradley K, Smith J R, Hatzopoulos A K, Knapik E W. The feelgood mutation in zebrafish dysregulates COPII-dependent secretion of select extracellular matrix proteins in skeletal morphogenesis. Dis Model Mech. 2011;4(6):763–776. doi: 10.1242/dmm.007625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  150. Menon A K, Vidugiriene J. Topology of GPI biosynthesis in the endoplasmic reticulum. Braz J Med Biol Res. 1994;27(2):167–175. [PubMed] [Google Scholar]
  151. Merulla J, Fasana E, Soldà T, Molinari M. Specificity and regulation of the endoplasmic reticulum-associated degradation machinery. Traffic. 2013;14(7):767–777. doi: 10.1111/tra.12068. [DOI] [PubMed] [Google Scholar]
  152. Meusser B, Hirsch C, Jarosch E, Sommer T. ERAD: the long road to destruction. Nat Cell Biol. 2005;7(8):766–772. doi: 10.1038/ncb0805-766. [DOI] [PubMed] [Google Scholar]
  153. Meyer H A, Hartmann E. The yeast SPC22/23 homolog Spc3p is essential for signal peptidase activity. J Biol Chem. 1997;272(20):13159–13164. doi: 10.1074/jbc.272.20.13159. [DOI] [PubMed] [Google Scholar]
  154. Miller E A, Schekman R. COPII- a flexible vesicle formation system. Curr Opin Cell Biol. 2013;25(4):420–427. doi: 10.1016/j.ceb.2013.04.005. [DOI] [PMC free article] [PubMed] [Google Scholar]
  155. Miller S E, Collins B M, McCoy A J, Robinson M S, Owen D J. A SNARE-adaptor interaction is a new mode of cargo recognition in clathrin-coated vesicles. Nature. 2007;450(7169):570–574. doi: 10.1038/nature06353. [DOI] [PubMed] [Google Scholar]
  156. Mironov A A, Beznoussenko G V, Nicoziani P, Martella O, Trucco A, Kweon H S, Di Giandomenico D, Polishchuk R S, Fusella A, Lupetti P, Berger E G, Geerts W J, Koster A J, Burger K N, Luini A. Small cargo proteins and large aggregates can traverse the Golgi by a common mechanism without leaving the lumen of cisternae. J Cell Biol. 2001;155(7):1225–1238. doi: 10.1083/jcb.200108073. [DOI] [PMC free article] [PubMed] [Google Scholar]
  157. Moore K A, Hollien J. The unfolded protein response in secretory cell function. Annu Rev Genet. 2012;46(1):165–183. doi: 10.1146/annurev-genet-110711-155644. [DOI] [PubMed] [Google Scholar]
  158. Mori K. Signalling pathways in the unfolded protein response: development from yeast to mammals. J Biochem. 2009;146(6):743–750. doi: 10.1093/jb/mvp166. [DOI] [PubMed] [Google Scholar]
  159. Mullins C, Meyer H A, Hartmann E, Green N, Fang H. Structurally related Spc1p and Spc2p of yeast signal peptidase complex are functionally distinct. J Biol Chem. 1996;271(46):29094–29099. doi: 10.1074/jbc.271.46.29094. [DOI] [PubMed] [Google Scholar]
  160. Murakami T, Kondo S, Ogata M, Kanemoto S, Saito A, Wanaka A, Imaizumi K. Cleavage of the membrane-bound transcription factor OASIS in response to endoplasmic reticulum stress. J Neurochem. 2006;96(4):1090–1100. doi: 10.1111/j.1471-4159.2005.03596.x. [DOI] [PubMed] [Google Scholar]
  161. Murakami T, Saito A, Hino S, Kondo S, Kanemoto S, Chihara K, Sekiya H, Tsumagari K, Ochiai K, Yoshinaga K, Saitoh M, Nishimura R, Yoneda T, Kou I, Furuichi T, Ikegawa S, Ikawa M, Okabe M, Wanaka A, Imaizumi K. Signalling mediated by the endoplasmic reticulum stress transducer OASIS is involved in bone formation. Nat Cell Biol. 2009;11(10):1205–1211. doi: 10.1038/ncb1963. [DOI] [PubMed] [Google Scholar]
  162. Naim H Y, Joberty G, Alfalah M, Jacob R. Temporal association of the N- and O-linked glycosylation events and their implication in the polarized sorting of intestinal brush border sucrase-isomaltase, aminopeptidase N, and dipeptidyl peptidase IV. J Biol Chem. 1999;274(25):17961–17967. doi: 10.1074/jbc.274.25.17961. [DOI] [PubMed] [Google Scholar]
  163. Nakamura N, Wei J H, Seemann J. Modular organization of the mammalian Golgi apparatus. Curr Opin Cell Biol. 2012;24(4):467–474. doi: 10.1016/j.ceb.2012.05.009. [DOI] [PMC free article] [PubMed] [Google Scholar]
  164. Ng D T, Brown J D, Walter P. Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J Cell Biol. 1996;134(2):269–278. doi: 10.1083/jcb.134.2.269. [DOI] [PMC free article] [PubMed] [Google Scholar]
  165. Ng D T, Walter P. Protein translocation across the endoplasmic reticulum. Curr Opin Cell Biol. 1994;6(4):510–516. doi: 10.1016/0955-0674(94)90069-8. [DOI] [PubMed] [Google Scholar]
  166. Nikaido T, Yokoya S, Mori T, Hagino S, Iseki K, Zhang Y, Takeuchi M, Takaki H, Kikuchi S, Wanaka A. Expression of the novel transcription factor OASIS, which belongs to the CREB/ATF family, in mouse embryo with special reference to bone development. Histochem Cell Biol. 2001;116(2):141–148. doi: 10.1007/s004180100279. [DOI] [PubMed] [Google Scholar]
  167. Nishikawa S, Nakano A. Identification of a gene required for membrane protein retention in the early secretory pathway. Proc Natl Acad Sci USA. 1993;90(17):8179–8183. doi: 10.1073/pnas.90.17.8179. [DOI] [PMC free article] [PubMed] [Google Scholar]
  168. Nyathi Y, Wilkinson B M, Pool M R. Co-translational targeting and translocation of proteins to the endoplasmic reticulum. Biochim Biophys Acta. 2013;1833(11):2392–2402. doi: 10.1016/j.bbamcr.2013.02.021. [DOI] [PubMed] [Google Scholar]
  169. Oka O B, Bulleid N J. Forming disulfides in the endoplasmic reticulum. Biochim Biophys Acta. 2013;1833(11):2425–2429. doi: 10.1016/j.bbamcr.2013.02.007. [DOI] [PubMed] [Google Scholar]
  170. Okada T, Yoshida H, Akazawa R, Negishi M, Mori K. Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response. Biochem J. 2002;366(Pt2):585–594. doi: 10.1042/BJ20020391. [DOI] [PMC free article] [PubMed] [Google Scholar]
  171. Olzmann J A, Kopito R R, Christianson J C. The mammalian endoplasmic reticulum-associated degradation system. Cold Spring Harb Perspect Biol. 2013;5(9):5. doi: 10.1101/cshperspect.a013185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  172. Omori Y, Imai J, Suzuki Y, Watanabe S, Tanigami A, Sugano S. OASIS is a transcriptional activator of CREB/ATF family with a transmembrane domain. Biochem Biophys Res Commun. 2002;293(1):470–477. doi: 10.1016/S0006-291X(02)00253-X. [DOI] [PubMed] [Google Scholar]
  173. Orlean P, Menon A K. Thematic review series: lipid posttranslational modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids. J Lipid Res. 2007;48(5):993–1011. doi: 10.1194/jlr.R700002-JLR200. [DOI] [PubMed] [Google Scholar]
  174. Osborne A R, Rapoport T A, van den Berg B. Protein translocation by the Sec61/SecY channel. Annu Rev Cell Dev Biol. 2005;21(1):529–550. doi: 10.1146/annurev.cellbio.21.012704.133214. [DOI] [PubMed] [Google Scholar]
  175. Panzner S, Dreier L, Hartmann E, Kostka S, Rapoport T A. Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell. 1995;81(4):561–570. doi: 10.1016/0092-8674(95)90077-2. [DOI] [PubMed] [Google Scholar]
  176. Papandreou I, Denko N C, Olson M, Van Melckebeke H, Lust S, Tam A, Solow-Cordero D E, Bouley D M, Offner F, Niwa M, Koong A C. Identification of an Ire1alpha endonuclease specific inhibitor with cytotoxic activity against human multiple myeloma. Blood. 2011;117(4):1311–1314. doi: 10.1182/blood-2010-08-303099. [DOI] [PMC free article] [PubMed] [Google Scholar]
  177. Pellett P A, Dietrich F, Bewersdorf J, Rothman J E, Lavieu G. Inter-Golgi transport mediated by COPI-containing vesicles carrying small cargoes. Elife. 2013;2:e01296. doi: 10.7554/eLife.01296. [DOI] [PMC free article] [PubMed] [Google Scholar]
  178. Pols MS, van Meel E, Oorschot V, ten Brink C, Fukuda M, Swetha MG, Mayor S, Klumperman J. hVps41 and VAMP7 function in direct TGN to late endosome transport of lysosomal membrane proteins. Nat Commun. 2013;4:1361. doi: 10.1038/ncomms2360. [DOI] [PubMed] [Google Scholar]
  179. Qi H, Fillion C, Labrie Y, Grenier J, Fournier A, Berger L, El-Alfy M, Labrie C. AIbZIP, a novel bZIP gene located on chromosome 1q21.3 that is highly expressed in prostate tumors and of which the expression is up-regulated by androgens in LNCaP human prostate cancer cells. Cancer Res. 2002;62(3):721–733. [PubMed] [Google Scholar]
  180. Quinn R S, Krane S M. Abnormal properties of collagen lysyl hydroxylase from skin fibroblasts of siblings with hydroxylysinedeficient collagen. J Clin Invest. 1976;57(1):83–93. doi: 10.1172/JCI108273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  181. Raden D, Song W, Gilmore R. Role of the cytoplasmic segments of Sec61alpha in the ribosome-binding and translocation-promoting activities of the Sec61 complex. J Cell Biol. 2000;150(1):53–64. doi: 10.1083/jcb.150.1.53. [DOI] [PMC free article] [PubMed] [Google Scholar]
  182. Rapoport T A. Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature. 2007;450(7170):663–669. doi: 10.1038/nature06384. [DOI] [PubMed] [Google Scholar]
  183. Reiling J H, Olive A J, Sanyal S, Carette J E, Brummelkamp T R, Ploegh H L, Starnbach M N, Sabatini D M. A CREB3-ARF4 signalling pathway mediates the response to Golgi stress and susceptibility to pathogens. Nat Cell Biol. 2013;15(12):1473–1485. doi: 10.1038/ncb2865. [DOI] [PMC free article] [PubMed] [Google Scholar]
  184. Rome M E, Rao M, Clemons W M, Shan S O. Precise timing of ATPase activation drives targeting of tail-anchored proteins. Proc Natl Acad Sci USA. 2013;110(19):7666–7671. doi: 10.1073/pnas.1222054110. [DOI] [PMC free article] [PubMed] [Google Scholar]
  185. Roth J, Wang Y, Eckhardt A E, Hill R L. Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland. Proc Natl Acad Sci USA. 1994;91(19):8935–8939. doi: 10.1073/pnas.91.19.8935. [DOI] [PMC free article] [PubMed] [Google Scholar]
  186. Ryoo H D, Domingos P M, Kang M J, Steller H. Unfolded protein response in a Drosophila model for retinal degeneration. EMBO J. 2007;26(1):242–252. doi: 10.1038/sj.emboj.7601477. [DOI] [PMC free article] [PubMed] [Google Scholar]
  187. Ryoo H D, Li J, Kang M J. Drosophila XBP1 expression reporter marks cells under endoplasmic reticulum stress and with high protein secretory load. PLoS ONE. 2013;8(9):e75774. doi: 10.1371/journal.pone.0075774. [DOI] [PMC free article] [PubMed] [Google Scholar]
  188. Saito A, Hino S, Murakami T, Kanemoto S, Kondo S, Saitoh M, Nishimura R, Yoneda T, Furuichi T, Ikegawa S, Ikawa M, Okabe M, Imaizumi K. Regulation of endoplasmic reticulum stress response by a BBF2H7-mediated Sec23a pathway is essential for chondrogenesis. Nat Cell Biol. 2009;11(10):1197–1204. doi: 10.1038/ncb1962. [DOI] [PubMed] [Google Scholar]
  189. Saito A, Kanemoto S, Kawasaki N, Asada R, Iwamoto H, Oki M, Miyagi H, Izumi S, Sanosaka T, Nakashima K, Imaizumi K. Unfolded protein response, activated by OASIS family transcription factors, promotes astrocyte differentiation. Nat Commun. 2012;3:967. doi: 10.1038/ncomms1971. [DOI] [PubMed] [Google Scholar]
  190. Saito A, Kanemoto S, Zhang Y, Asada R, Hino K, Imaizumi K. Chondrocyte proliferation regulated by secreted luminal domain of ER stress transducer BBF2H7/CREB3L2. Mol Cell. 2014;53(1):127–139. doi: 10.1016/j.molcel.2013.11.008. [DOI] [PubMed] [Google Scholar]
  191. Sanecka A, Ansems M, van Hout-Kuijer M A, Looman M W, Prosser A C, Welten S, Gilissen C, Sama I E, Huynen MA, Veltman J A, Jansen B J, Eleveld-Trancikova D, Adema G J. Analysis of genes regulated by the transcription factor LUMAN identifies ApoA4 as a target gene in dendritic cells. Mol Immunol. 2012;50(1–2):66–73. doi: 10.1016/j.molimm.2011.12.003. [DOI] [PubMed] [Google Scholar]
  192. Saraogi I, Shan S O. Molecular mechanism of co-translational protein targeting by the signal recognition particle. Traffic. 2011;12(5):535–542. doi: 10.1111/j.1600-0854.2011.01171.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  193. Sato K, Sato M, Nakano A. Rer1p, a retrieval receptor for ER membrane proteins, recognizes transmembrane domains in multiple modes. Mol Biol Cell. 2003;14(9):3605–3616. doi: 10.1091/mbc.E02-12-0777. [DOI] [PMC free article] [PubMed] [Google Scholar]
  194. Schnell D J, Hebert D N. Protein translocons: multifunctional mediators of protein translocation across membranes. Cell. 2003;112(4):491–505. doi: 10.1016/s0092-8674(03)00110-7. [DOI] [PubMed] [Google Scholar]
  195. Schuldiner M, Metz J, Schmid V, Denic V, Rakwalska M, Schmitt H D, Schwappach B, Weissman J S. The GET complex mediates insertion of tail-anchored proteins into the ER membrane. Cell. 2008;134(4):634–645. doi: 10.1016/j.cell.2008.06.025. [DOI] [PMC free article] [PubMed] [Google Scholar]
  196. Schweizer A, Stahl P D, Rohrer J. A di-aromatic motif in the cytosolic tail of the mannose receptor mediates endosomal sorting. J Biol Chem. 2000;275(38):29694–29700. doi: 10.1074/jbc.M000571200. [DOI] [PubMed] [Google Scholar]
  197. Semenza J C, Hardwick K G, Dean N, Pelham H R. ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell. 1990;61(7):1349–1357. doi: 10.1016/0092-8674(90)90698-e. [DOI] [PubMed] [Google Scholar]
  198. Shaffer A L, Shapiro-Shelef M, Iwakoshi N N, Lee A H, Qian S B, Zhao H, Yu X, Yang L, Tan B K, Rosenwald A, Hurt E M, Petroulakis E, Sonenberg N, Yewdell J W, Calame K, Glimcher L H, Staudt L M. XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation. Immunity. 2004;21(1):81–93. doi: 10.1016/j.immuni.2004.06.010. [DOI] [PubMed] [Google Scholar]
  199. Shao S, Hegde R S. A calmodulin-dependent translocation pathway for small secretory proteins. Cell. 2011;147(7):1576–1588. doi: 10.1016/j.cell.2011.11.048. [DOI] [PMC free article] [PubMed] [Google Scholar]
  200. Shao S, Hegde R S. Membrane protein insertion at the endoplasmic reticulum. Annu Rev Cell Dev Biol. 2011;27(1):25–56. doi: 10.1146/annurev-cellbio-092910-154125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  201. Smolik SM, Rose R E, Goodman R H. A cyclic AMP-responsive element-binding transcriptional activator in Drosophila melanogaster, dCREB-A, is a member of the leucine zipper family. Mol Cell Biol. 1992;12(9):4123–4131. doi: 10.1128/mcb.12.9.4123. [DOI] [PMC free article] [PubMed] [Google Scholar]
  202. Sone M, Zeng X, Larese J, Ryoo H D. A modified UPR stress sensing system reveals a novel tissue distribution of IRE1/XBP1 activity during normal Drosophila development. Cell Stress Chaperones. 2013;18(3):307–319. doi: 10.1007/s12192-012-0383-x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  203. Song W, Raden D, Mandon E C, Gilmore R. Role of Sec61alpha in the regulated transfer of the ribosome-nascent chain complex from the signal recognition particle to the translocation channel. Cell. 2000;100(3):333–343. doi: 10.1016/s0092-8674(00)80669-8. [DOI] [PubMed] [Google Scholar]
  204. Souid S, Lepesant J A, Yanicostas C. The xbp-1 gene is essential for development in Drosophila. Dev Genes Evol. 2007;217(2):159–167. doi: 10.1007/s00427-006-0124-1. [DOI] [PubMed] [Google Scholar]
  205. Sousa M C, Ferrero-Garcia M A, Parodi A J. Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDPGlc: glycoprotein glucosyltransferase. Biochemistry. 1992;31(1):97–105. doi: 10.1021/bi00116a015. [DOI] [PubMed] [Google Scholar]
  206. Spiro R G. Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology. 2002;12(4):43R–56R. doi: 10.1093/glycob/12.4.43r. [DOI] [PubMed] [Google Scholar]
  207. Sriburi R, Jackowski S, Mori K, Brewer J W. XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum. J Cell Biol. 2004;167(1):35–41. doi: 10.1083/jcb.200406136. [DOI] [PMC free article] [PubMed] [Google Scholar]
  208. Stefanovic S, Hegde R S. Identification of a targeting factor for posttranslational membrane protein insertion into the ER. Cell. 2007;128(6):1147–1159. doi: 10.1016/j.cell.2007.01.036. [DOI] [PubMed] [Google Scholar]
  209. Stefer S, Reitz S, Wang F, Wild K, Pang Y Y, Schwarz D, Bomke J, Hein C, Löhr F, Bernhard F, Denic V, Dötsch V, Sinning I. Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex. Science. 2011;333(6043):758–762. doi: 10.1126/science.1207125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  210. Stirling J, O’hare P. CREB4, a transmembrane bZip transcription factor and potential new substrate for regulation and cleavage by S1P. Mol Biol Cell. 2006;17(1):413–426. doi: 10.1091/mbc.E05-06-0500. [DOI] [PMC free article] [PubMed] [Google Scholar]
  211. Storlazzi C T, Mertens F, Nascimento A, Isaksson M, Wejde J, Brosjo O, Mandahl N, Panagopoulos I. Fusion of the FUS and BBF2H7 genes in low grade fibromyxoid sarcoma. Hum Mol Genet. 2003;12(18):2349–2358. doi: 10.1093/hmg/ddg237. [DOI] [PubMed] [Google Scholar]
  212. Strating J R, van Bakel N H, Leunissen J A, Martens G J. A comprehensive overview of the vertebrate p24 family: identification of a novel tissue-specifically expressed member. Mol Biol Evol. 2009;26(8):1707–1714. doi: 10.1093/molbev/msp099. [DOI] [PubMed] [Google Scholar]
  213. Suh J, Hutter H. A survey of putative secreted and transmembrane proteins encoded in the C. elegans genome. BMC Genomics. 2012;13(1):333. doi: 10.1186/1471-2164-13-333. [DOI] [PMC free article] [PubMed] [Google Scholar]
  214. Tanegashima K, Zhao H, Rebbert M L, Dawid I B. Coordinated activation of the secretory pathway during notochord formation in the Xenopus embryo. Development. 2009;136(21):3543–3548. doi: 10.1242/dev.036715. [DOI] [PMC free article] [PubMed] [Google Scholar]
  215. Taubenheim N, Tarlinton D M, Crawford S, Corcoran L M, Hodgkin P D, Nutt S L. High rate of antibody secretion is not integral to plasma cell differentiation as revealed by XBP-1 deficiency. J Immunol. 2012;189(7):3328–3338. doi: 10.4049/jimmunol.1201042. [DOI] [PubMed] [Google Scholar]
  216. Thibault G, Ng D T. The endoplasmic reticulum-associated degradation pathways of budding yeast. Cold Spring Harb Perspect Biol. 2012;4(12):4. doi: 10.1101/cshperspect.a013193. [DOI] [PMC free article] [PubMed] [Google Scholar]
  217. Todd D J, Lee A H, Glimcher L H. The endoplasmic reticulum stress response in immunity and autoimmunity. Nat Rev Immunol. 2008;8(9):663–674. doi: 10.1038/nri2359. [DOI] [PubMed] [Google Scholar]
  218. Tohmonda T, Miyauchi Y, Ghosh R, Yoda M, Uchikawa S, Takito J, Morioka H, Nakamura M, Iwawaki T, Chiba K, Toyama Y, Urano F, Horiuchi K. The IRE1α-XBP1 pathway is essential for osteoblast differentiation through promoting transcription of Osterix. EMBO Rep. 2011;12(5):451–457. doi: 10.1038/embor.2011.34. [DOI] [PMC free article] [PubMed] [Google Scholar]
  219. Townsley FM, Pelham H R. The KKXX signal mediates retrieval of membrane proteins from the Golgi to the ER in yeast. Eur J Cell Biol. 1994;64(1):211–216. [PubMed] [Google Scholar]
  220. Travers K J, Patil C K, Wodicka L, Lockhart D J, Weissman J S, Walter P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER associated degradation. Cell. 2000;101(3):249–258. doi: 10.1016/s0092-8674(00)80835-1. [DOI] [PubMed] [Google Scholar]
  221. Ungar D, Oka T, Brittle E E, Vasile E, Lupashin V V, Chatterton J E, Heuser J E, Krieger M, Waters M G. Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function. J Cell Biol. 2002;157(3):405–415. doi: 10.1083/jcb.200202016. [DOI] [PMC free article] [PubMed] [Google Scholar]
  222. Valdés P, Mercado G, Vidal R L, Molina C, Parsons G, Court F A, Martinez A, Galleguillos D, Armentano D, Schneider B L, Hetz C. Control of dopaminergic neuron survival by the unfolded protein response transcription factor XBP1. Proc Natl Acad Sci USA. 2014;111(18):6804–6809. doi: 10.1073/pnas.1321845111. [DOI] [PMC free article] [PubMed] [Google Scholar]
  223. Vecchi C, Montosi G, Zhang K, Lamberti I, Duncan S A, Kaufman R J, Pietrangelo A. ER stress controls iron metabolism through induction of hepcidin. Science. 2009;325(5942):877–880. doi: 10.1126/science.1176639. [DOI] [PMC free article] [PubMed] [Google Scholar]
  224. Vellanki R N, Zhang L, Guney MA, Rocheleau J V, Gannon M, Volchuk A. OASIS/CREB3L1 induces expression of genes involved in extracellular matrix production but not classical endoplasmic reticulum stress response genes in pancreatic beta-cells. Endocrinology. 2010;151(9):4146–4157. doi: 10.1210/en.2010-0137. [DOI] [PMC free article] [PubMed] [Google Scholar]
  225. Venditti R, Wilson C, De Matteis M A. Exiting the ER: what we know and what we don’t. Trends Cell Biol. 2014;24(1):9–18. doi: 10.1016/j.tcb.2013.08.005. [DOI] [PubMed] [Google Scholar]
  226. Vidugiriene J, Menon A K. The GPI anchor of cell-surface proteins is synthesized on the cytoplasmic face of the endoplasmic reticulum. J Cell Biol. 1994;127(2):333–341. doi: 10.1083/jcb.127.2.333. [DOI] [PMC free article] [PubMed] [Google Scholar]
  227. Volkmann K, Lucas J L, Vuga D, Wang X, Brumm D, Stiles C, Kriebel D, Der-Sarkissian A, Krishnan K, Schweitzer C, Liu Z, Malyankar U M, Chiovitti D, Canny M, Durocher D, Sicheri F, Patterson J B. Potent and selective inhibitors of the inositol-requiring enzyme 1 endoribonuclease. J Biol Chem. 2011;286(14):12743–12755. doi: 10.1074/jbc.M110.199737. [DOI] [PMC free article] [PubMed] [Google Scholar]
  228. von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem. 1983;133(1):17–21. doi: 10.1111/j.1432-1033.1983.tb07424.x. [DOI] [PubMed] [Google Scholar]
  229. Walter P, Blobel G. Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes. J Cell Biol. 1981;91(2Pt1):557–561. doi: 10.1083/jcb.91.2.557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  230. Walter P, Blobel G. Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum. Nature. 1982;299(5885):691–698. doi: 10.1038/299691a0. [DOI] [PubMed] [Google Scholar]
  231. Walter P, Johnson A E. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu Rev Cell Biol. 1994;10(1):87–119. doi: 10.1146/annurev.cb.10.110194.000511. [DOI] [PubMed] [Google Scholar]
  232. Wang F, Brown E C, Mak G, Zhuang J, Denic V. A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol Cell. 2010;40(1):159–171. doi: 10.1016/j.molcel.2010.08.038. [DOI] [PMC free article] [PubMed] [Google Scholar]
  233. Wereszczynski J, McCammon J A. Nucleotide-dependent mechanism of Get3 as elucidated from free energy calculations. Proc Natl Acad Sci USA. 2012;109(20):7759–7764. doi: 10.1073/pnas.1117441109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  234. Willett R, Kudlyk T, Pokrovskaya I, Schönherr R, Ungar D, Duden R, Lupashin V. COG complexes form spatial landmarks for distinct SNARE complexes. Nat Commun. 2013;4:1553. doi: 10.1038/ncomms2535. [DOI] [PMC free article] [PubMed] [Google Scholar]
  235. Willett R, Ungar D, Lupashin V. The Golgi puppet master: COG complex at center stage of membrane trafficking interactions. Histochem Cell Biol. 2013;140(3):271–283. doi: 10.1007/s00418-013-1117-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  236. Williams D B. Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum. J Cell Sci. 2006;119(Pt4):615–623. doi: 10.1242/jcs.02856. [DOI] [PubMed] [Google Scholar]
  237. Wu J, Rutkowski D T, Dubois M, Swathirajan J, Saunders T, Wang J, Song B, Yau G D, Kaufman R J. ATF6alpha optimizes longterm endoplasmic reticulum function to protect cells from chronic stress. Dev Cell. 2007;13(3):351–364. doi: 10.1016/j.devcel.2007.07.005. [DOI] [PubMed] [Google Scholar]
  238. Xu X, Park J G, So J S, Hur K Y, Lee A H. Transcriptional regulation of apolipoprotein A-IV by the transcription factor CREBH. J Lipid Res. 2014;55(5):850–859. doi: 10.1194/jlr.M045104. [DOI] [PMC free article] [PubMed] [Google Scholar]
  239. YaDeau J T, Klein C, Blobel G. Yeast signal peptidase contains a glycoprotein and the Sec11 gene product. Proc Natl Acad Sci USA. 1991;88(2):517–521. doi: 10.1073/pnas.88.2.517. [DOI] [PMC free article] [PubMed] [Google Scholar]
  240. Yamamoto K, Sato T, Matsui T, Sato M, Okada T, Yoshida H, Harada A, Mori K. Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1. Dev Cell. 2007;13(3):365–376. doi: 10.1016/j.devcel.2007.07.018. [DOI] [PubMed] [Google Scholar]
  241. Yoshida H, Haze K, Yanagi H, Yura T, Mori K. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucoseregulated proteins. Involvement of basic leucine zipper transcription factors. J Biol Chem. 1998;273(50):33741–33749. doi: 10.1074/jbc.273.50.33741. [DOI] [PubMed] [Google Scholar]
  242. Yoshida H, Matsui T, Yamamoto A, Okada T, Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell. 2001;107(7):881–891. doi: 10.1016/s0092-8674(01)00611-0. [DOI] [PubMed] [Google Scholar]
  243. Yoshizawa T, Hinoi E, Jung D Y, Kajimura D, Ferron M, Seo J, Graff J M, Kim J K, Karsenty G. The transcription factor ATF4 regulates glucose metabolism in mice through its expression in osteoblasts. J Clin Invest. 2009;119(9):2807–2817. doi: 10.1172/JCI39366. [DOI] [PMC free article] [PubMed] [Google Scholar]
  244. Young B P, Craven R A, Reid P J, Willer M, Stirling C J. Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo. EMBO J. 2001;20(1–2):262–271. doi: 10.1093/emboj/20.1.262. [DOI] [PMC free article] [PubMed] [Google Scholar]
  245. Zanetti G, Pahuja K B, Studer S, Shim S, Schekman R. COPII and the regulation of protein sorting in mammals. Nat Cell Biol. 2012;14(1):20–28. doi: 10.1038/ncb2390. [DOI] [PubMed] [Google Scholar]
  246. Zanna P T, Sánchez-Laorden B L, Pérez-Oliva A B, Turpín MC, Herraiz C, Jiménez-Cervantes C, García-Borrón J C. Mechanism of dimerization of the human melanocortin 1 receptor. Biochem Biophys Res Commun. 2008;368(2):211–216. doi: 10.1016/j.bbrc.2008.01.060. [DOI] [PubMed] [Google Scholar]
  247. Zhang C, Bai N, Chang A, Zhang Z, Yin J, Shen W, Tian Y, Xiang R, Liu C. ATF4 is directly recruited by TLR4 signaling and positively regulates TLR4-trigged cytokine production in human monocytes. Cell Mol Immunol. 2013;10(1):84–94. doi: 10.1038/cmi.2012.57. [DOI] [PMC free article] [PubMed] [Google Scholar]
  248. Zhang K, Shen X, Wu J, Sakaki K, Saunders T, Rutkowski D T, Back S H, Kaufman R J. Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell. 2006;124(3):587–599. doi: 10.1016/j.cell.2005.11.040. [DOI] [PubMed] [Google Scholar]

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