Skip to main content
PMC home page
The Plant Cell logoLink to The Plant Cell
. 1999 Apr;11(4):615–628. doi: 10.1105/tpc.11.4.615

The endoplasmic reticulum-gateway of the secretory pathway

A Vitale 1, J Denecke 1
PMCID: PMC144197  PMID: 10213782

Full Text

The Full Text of this article is available as a PDF (212.9 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Akasofu H., Yamauchi D., Mitsuhashi W., Minamikawa T. Nucleotide sequence of cDNA for sulfhydryl-endopeptidase (SH-EP) from cotyledons of germinating Vigna mungo seeds. Nucleic Acids Res. 1989 Aug 25;17(16):6733–6733. doi: 10.1093/nar/17.16.6733. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bagga S., Adams H. P., Rodriguez F. D., Kemp J. D., Sengupta-Gopalan C. Coexpression of the maize delta-zein and beta-zein genes results in stable accumulation of delta-zein in endoplasmic reticulum-derived protein bodies formed by beta-zein. Plant Cell. 1997 Sep;9(9):1683–1696. doi: 10.1105/tpc.9.9.1683. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Balch W. E., McCaffery J. M., Plutner H., Farquhar M. G. Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum. Cell. 1994 Mar 11;76(5):841–852. doi: 10.1016/0092-8674(94)90359-x. [DOI] [PubMed] [Google Scholar]
  4. Bar-Peled M., Conceicao AdS., Frigerio L., Raikhel N. V. Expression and Regulation of aERD2, a Gene Encoding the KDEL Receptor Homolog in Plants, and Other Genes Encoding Proteins Involved in ER-Golgi Vesicular Trafficking. Plant Cell. 1995 Jun;7(6):667–676. doi: 10.1105/tpc.7.6.667. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Barlowe C., Orci L., Yeung T., Hosobuchi M., Hamamoto S., Salama N., Rexach M. F., Ravazzola M., Amherdt M., Schekman R. COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell. 1994 Jun 17;77(6):895–907. doi: 10.1016/0092-8674(94)90138-4. [DOI] [PubMed] [Google Scholar]
  6. Battey NH, James NC, Greenland AJ, Brownlee C. Exocytosis and endocytosis . Plant Cell. 1999 Apr;11(4):643–660. doi: 10.1105/tpc.11.4.643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Bednarek S. Y., Wilkins T. A., Dombrowski J. E., Raikhel N. V. A carboxyl-terminal propeptide is necessary for proper sorting of barley lectin to vacuoles of tobacco. Plant Cell. 1990 Dec;2(12):1145–1155. doi: 10.1105/tpc.2.12.1145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Boevink P., Oparka K., Santa Cruz S., Martin B., Betteridge A., Hawes C. Stacks on tracks: the plant Golgi apparatus traffics on an actin/ER network. Plant J. 1998 Aug;15(3):441–447. doi: 10.1046/j.1365-313x.1998.00208.x. [DOI] [PubMed] [Google Scholar]
  9. Boston R. S., Fontes E. B., Shank B. B., Wrobel R. L. Increased expression of the maize immunoglobulin binding protein homolog b-70 in three zein regulatory mutants. Plant Cell. 1991 May;3(5):497–505. doi: 10.1105/tpc.3.5.497. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Boston R. S., Viitanen P. V., Vierling E. Molecular chaperones and protein folding in plants. Plant Mol Biol. 1996 Oct;32(1-2):191–222. doi: 10.1007/BF00039383. [DOI] [PubMed] [Google Scholar]
  11. Braakman I., Helenius J., Helenius A. Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature. 1992 Mar 19;356(6366):260–262. doi: 10.1038/356260a0. [DOI] [PubMed] [Google Scholar]
  12. Calnexin, calreticulin and the folding of glycoproteins. Trends Cell Biol. 1997 May;7(5):193–200. doi: 10.1016/S0962-8924(97)01032-5. [DOI] [PubMed] [Google Scholar]
  13. Chrispeels M. J., Higgins T. J., Spencer D. Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons. J Cell Biol. 1982 May;93(2):306–313. doi: 10.1083/jcb.93.2.306. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Coleman C. E., Clore A. M., Ranch J. P., Higgins R., Lopes M. A., Larkins B. A. Expression of a mutant alpha-zein creates the floury2 phenotype in transgenic maize. Proc Natl Acad Sci U S A. 1997 Jun 24;94(13):7094–7097. doi: 10.1073/pnas.94.13.7094. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Coleman C. E., Herman E. M., Takasaki K., Larkins B. A. The maize gamma-zein sequesters alpha-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm. Plant Cell. 1996 Dec;8(12):2335–2345. doi: 10.1105/tpc.8.12.2335. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Coleman C. E., Lopes M. A., Gillikin J. W., Boston R. S., Larkins B. A. A defective signal peptide in the maize high-lysine mutant floury 2. Proc Natl Acad Sci U S A. 1995 Jul 18;92(15):6828–6831. doi: 10.1073/pnas.92.15.6828. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Cosson P., Letourneur F. Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science. 1994 Mar 18;263(5153):1629–1631. doi: 10.1126/science.8128252. [DOI] [PubMed] [Google Scholar]
  18. Crofts AJ, Leborgne-Castel N, Pesca M, Vitale A, Denecke J. BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress . Plant Cell. 1998 May;10(5):813–824. doi: 10.1105/tpc.10.5.813. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Crowley K. S., Reinhart G. D., Johnson A. E. The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation. Cell. 1993 Jun 18;73(6):1101–1115. doi: 10.1016/0092-8674(93)90640-c. [DOI] [PubMed] [Google Scholar]
  20. Denecke J., Botterman J., Deblaere R. Protein secretion in plant cells can occur via a default pathway. Plant Cell. 1990 Jan;2(1):51–59. doi: 10.1105/tpc.2.1.51. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Denecke J., Carlsson L. E., Vidal S., Höglund A. S., Ek B., van Zeijl M. J., Sinjorgo K. M., Palva E. T. The tobacco homolog of mammalian calreticulin is present in protein complexes in vivo. Plant Cell. 1995 Apr;7(4):391–406. doi: 10.1105/tpc.7.4.391. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Denecke J., De Rycke R., Botterman J. Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope. EMBO J. 1992 Jun;11(6):2345–2355. doi: 10.1002/j.1460-2075.1992.tb05294.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Dickinson C. D., Floener L. A., Lilley G. G., Nielsen N. C. Self-assembly of proglycinin and hybrid proglycinin synthesized in vitro from cDNA. Proc Natl Acad Sci U S A. 1987 Aug;84(16):5525–5529. doi: 10.1073/pnas.84.16.5525. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Fiedler K., Simons K. The role of N-glycans in the secretory pathway. Cell. 1995 May 5;81(3):309–312. doi: 10.1016/0092-8674(95)90380-1. [DOI] [PubMed] [Google Scholar]
  25. Frigerio L., Vitale A., Lord J. M., Ceriotti A., Roberts L. M. Free ricin A chain, proricin, and native toxin have different cellular fates when expressed in tobacco protoplasts. J Biol Chem. 1998 Jun 5;273(23):14194–14199. doi: 10.1074/jbc.273.23.14194. [DOI] [PubMed] [Google Scholar]
  26. Frigerio L., de Virgilio M., Prada A., Faoro F., Vitale A. Sorting of phaseolin to the vacuole is saturable and requires a short C-terminal peptide. Plant Cell. 1998 Jun;10(6):1031–1042. doi: 10.1105/tpc.10.6.1031. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Gillikin J. W., Zhang F., Coleman C. E., Bass H. W., Larkins B. A., Boston R. S. A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane. Plant Physiol. 1997 May;114(1):345–352. doi: 10.1104/pp.114.1.345. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Gomez L., Chrispeels M. J. Tonoplast and Soluble Vacuolar Proteins Are Targeted by Different Mechanisms. Plant Cell. 1993 Sep;5(9):1113–1124. doi: 10.1105/tpc.5.9.1113. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Haas I. G., Wabl M. Immunoglobulin heavy chain binding protein. Nature. 1983 Nov 24;306(5941):387–389. doi: 10.1038/306387a0. [DOI] [PubMed] [Google Scholar]
  30. 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 Mar 20;92(6):747–758. doi: 10.1016/s0092-8674(00)81403-8. [DOI] [PubMed] [Google Scholar]
  31. Hammond C., Braakman I., Helenius A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci U S A. 1994 Feb 1;91(3):913–917. doi: 10.1073/pnas.91.3.913. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Hammond C., Helenius A. Quality control in the secretory pathway. Curr Opin Cell Biol. 1995 Aug;7(4):523–529. doi: 10.1016/0955-0674(95)80009-3. [DOI] [PubMed] [Google Scholar]
  33. Hammond C., Helenius A. Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J Cell Biol. 1994 Jul;126(1):41–52. doi: 10.1083/jcb.126.1.41. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Hara-Nishimura I, Shimada T, Hatano K, Takeuchi Y, Nishimura M. Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles . Plant Cell. 1998 May;10(5):825–836. doi: 10.1105/tpc.10.5.825. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Hartl F. U. Molecular chaperones in cellular protein folding. Nature. 1996 Jun 13;381(6583):571–579. doi: 10.1038/381571a0. [DOI] [PubMed] [Google Scholar]
  36. Hellman R., Vanhove M., Lejeune A., Stevens F. J., Hendershot L. M. The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP. J Cell Biol. 1999 Jan 11;144(1):21–30. doi: 10.1083/jcb.144.1.21. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Henderson J., Bauly J. M., Ashford D. A., Oliver S. C., Hawes C. R., Lazarus C. M., Venis M. A., Napier R. M. Retention of maize auxin-binding protein in the endoplasmic reticulum: quantifying escape and the role of auxin. Planta. 1997;202(3):313–323. doi: 10.1007/s004250050133. [DOI] [PubMed] [Google Scholar]
  38. Herman EM, Larkins BA. Protein storage bodies and vacuoles . Plant Cell. 1999 Apr;11(4):601–614. doi: 10.1105/tpc.11.4.601. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Hiller M. M., Finger A., Schweiger M., Wolf D. H. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science. 1996 Sep 20;273(5282):1725–1728. doi: 10.1126/science.273.5282.1725. [DOI] [PubMed] [Google Scholar]
  40. Holkeri H., Makarow M. Different degradation pathways for heterologous glycoproteins in yeast. FEBS Lett. 1998 Jun 12;429(2):162–166. doi: 10.1016/s0014-5793(98)00586-9. [DOI] [PubMed] [Google Scholar]
  41. Hong E., Davidson A. R., Kaiser C. A. A pathway for targeting soluble misfolded proteins to the yeast vacuole. J Cell Biol. 1996 Nov;135(3):623–633. doi: 10.1083/jcb.135.3.623. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Hunt D. C., Chrispeels M. J. The signal Peptide of a vacuolar protein is necessary and sufficient for the efficient secretion of a cytosolic protein. Plant Physiol. 1991 May;96(1):18–25. doi: 10.1104/pp.96.1.18. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Hurtley S. M., Helenius A. Protein oligomerization in the endoplasmic reticulum. Annu Rev Cell Biol. 1989;5:277–307. doi: 10.1146/annurev.cb.05.110189.001425. [DOI] [PubMed] [Google Scholar]
  44. Hwang C., Sinskey A. J., Lodish H. F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science. 1992 Sep 11;257(5076):1496–1502. doi: 10.1126/science.1523409. [DOI] [PubMed] [Google Scholar]
  45. Inohara N., Shimomura S., Fukui T., Futai M. Auxin-binding protein located in the endoplasmic reticulum of maize shoots: molecular cloning and complete primary structure. Proc Natl Acad Sci U S A. 1989 May;86(10):3564–3568. doi: 10.1073/pnas.86.10.3564. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Jiang L., Rogers J. C. Integral membrane protein sorting to vacuoles in plant cells: evidence for two pathways. J Cell Biol. 1998 Nov 30;143(5):1183–1199. doi: 10.1083/jcb.143.5.1183. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Jung R., Nam Y. W., Saalbach I., Müntz K., Nielsen N. C. Role of the sulfhydryl redox state and disulfide bonds in processing and assembly of 11S seed globulins. Plant Cell. 1997 Nov;9(11):2037–2050. doi: 10.1105/tpc.9.11.2037. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Kermode A. R., Fisher S. A., Polishchuk E., Wandelt C., Spencer D., Higgins T. J. Accumulation and proteolytic processing of vicilin deletion-mutant proteins in the leaf and seed of transgenic tobacco. Planta. 1995;197(3):501–513. doi: 10.1007/BF00196672. [DOI] [PubMed] [Google Scholar]
  49. Kim J. H., Johannes L., Goud B., Antony C., Lingwood C. A., Daneman R., Grinstein S. Noninvasive measurement of the pH of the endoplasmic reticulum at rest and during calcium release. Proc Natl Acad Sci U S A. 1998 Mar 17;95(6):2997–3002. doi: 10.1073/pnas.95.6.2997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Leborgne-Castel N., Jelitto-Van Dooren E. P., Crofts A. J., Denecke J. Overexpression of BiP in tobacco alleviates endoplasmic reticulum stress. Plant Cell. 1999 Mar;11(3):459–470. doi: 10.1105/tpc.11.3.459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Levanony H., Rubin R., Altschuler Y., Galili G. Evidence for a novel route of wheat storage proteins to vacuoles. J Cell Biol. 1992 Dec;119(5):1117–1128. doi: 10.1083/jcb.119.5.1117. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Lewis M. J., Pelham H. R. Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum. Cell. 1992 Jan 24;68(2):353–364. doi: 10.1016/0092-8674(92)90476-s. [DOI] [PubMed] [Google Scholar]
  53. Li C. P., Larkins B. A. Expression of protein disulfide isomerase is elevated in the endosperm of the maize floury-2 mutant. Plant Mol Biol. 1996 Mar;30(5):873–882. doi: 10.1007/BF00020800. [DOI] [PubMed] [Google Scholar]
  54. Li X., Su R. T., Hsu H. T., Sze H. The molecular chaperone calnexin associates with the vacuolar H(+)-ATPase from oat seedlings. Plant Cell. 1998 Jan;10(1):119–130. doi: 10.1105/tpc.10.1.119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Li X., Wu Y., Zhang D. Z., Gillikin J. W., Boston R. S., Franceschi V. R., Okita T. W. Rice prolamine protein body biogenesis: a BiP-mediated process. Science. 1993 Nov 12;262(5136):1054–1056. doi: 10.1126/science.8235623. [DOI] [PubMed] [Google Scholar]
  56. Lippincott-Schwartz J., Bonifacino J. S., Yuan L. C., Klausner R. D. Degradation from the endoplasmic reticulum: disposing of newly synthesized proteins. Cell. 1988 Jul 15;54(2):209–220. doi: 10.1016/0092-8674(88)90553-3. [DOI] [PubMed] [Google Scholar]
  57. Lupattelli F., Pedrazzini E., Bollini R., Vitale A., Ceriotti A. The Rate of Phaseolin Assembly Is Controlled by the Glucosylation State of Its N-Linked Oligosaccharide Chains. Plant Cell. 1997 Apr;9(4):597–609. doi: 10.1105/tpc.9.4.597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Ma J. K., Hiatt A., Hein M., Vine N. D., Wang F., Stabila P., van Dolleweerd C., Mostov K., Lehner T. Generation and assembly of secretory antibodies in plants. Science. 1995 May 5;268(5211):716–719. doi: 10.1126/science.7732380. [DOI] [PubMed] [Google Scholar]
  59. Ma J. K., Hikmat B. Y., Wycoff K., Vine N. D., Chargelegue D., Yu L., Hein M. B., Lehner T. Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans. Nat Med. 1998 May;4(5):601–606. doi: 10.1038/nm0598-601. [DOI] [PubMed] [Google Scholar]
  60. Marty F. Plant vacuoles . Plant Cell. 1999 Apr;11(4):587–600. doi: 10.1105/tpc.11.4.587. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Muench D. G., Wu Y., Zhang Y., Li X., Boston R. S., Okita T. W. Molecular cloning, expression and subcellular localization of a BiP homolog from rice endosperm tissue. Plant Cell Physiol. 1997 Apr;38(4):404–412. doi: 10.1093/oxfordjournals.pcp.a029183. [DOI] [PubMed] [Google Scholar]
  62. Munro S., Pelham H. R. A C-terminal signal prevents secretion of luminal ER proteins. Cell. 1987 Mar 13;48(5):899–907. doi: 10.1016/0092-8674(87)90086-9. [DOI] [PubMed] [Google Scholar]
  63. Munro S., Pelham H. R. An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell. 1986 Jul 18;46(2):291–300. doi: 10.1016/0092-8674(86)90746-4. [DOI] [PubMed] [Google Scholar]
  64. Nam Y. W., Jung R., Nielsen N. C. Adenosine 5'-triphosphate is required for the assembly of 11S seed proglobulins in vitro. Plant Physiol. 1997 Dec;115(4):1629–1639. doi: 10.1104/pp.115.4.1629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Neuhaus J. M., Pietrzak M., Boller T. Mutation analysis of the C-terminal vacuolar targeting peptide of tobacco chitinase: low specificity of the sorting system, and gradual transition between intracellular retention and secretion into the extracellular space. Plant J. 1994 Jan;5(1):45–54. doi: 10.1046/j.1365-313x.1994.5010045.x. [DOI] [PubMed] [Google Scholar]
  66. Nishimura N., Balch W. E. A di-acidic signal required for selective export from the endoplasmic reticulum. Science. 1997 Jul 25;277(5325):556–558. doi: 10.1126/science.277.5325.556. [DOI] [PubMed] [Google Scholar]
  67. Okamoto T., Nakayama H., Seta K., Isobe T., Minamikawa T. Posttranslational processing of a carboxy-terminal propeptide containing a KDEL sequence of plant vacuolar cysteine endopeptidase (SH-EP) FEBS Lett. 1994 Aug 29;351(1):31–34. doi: 10.1016/0014-5793(94)00809-4. [DOI] [PubMed] [Google Scholar]
  68. Palade G. Intracellular aspects of the process of protein synthesis. Science. 1975 Aug 1;189(4200):347–358. doi: 10.1126/science.1096303. [DOI] [PubMed] [Google Scholar]
  69. Parodi A. J., Mendelzon D. H., Lederkremer G. Z., Martin-Barrientos J. Evidence that transient glucosylation of protein-linked Man9GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2 occurs in rat liver and Phaseolus vulgaris cells. J Biol Chem. 1984 May 25;259(10):6351–6357. [PubMed] [Google Scholar]
  70. Patterson S. I., Skene J. H. Novel inhibitory action of tunicamycin homologues suggests a role for dynamic protein fatty acylation in growth cone-mediated neurite extension. J Cell Biol. 1994 Feb;124(4):521–536. doi: 10.1083/jcb.124.4.521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. Pedrazzini E., Giovinazzo G., Bielli A., de Virgilio M., Frigerio L., Pesca M., Faoro F., Bollini R., Ceriotti A., Vitale A. Protein quality control along the route to the plant vacuole. Plant Cell. 1997 Oct;9(10):1869–1880. doi: 10.1105/tpc.9.10.1869. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Pelham H. R. Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment. EMBO J. 1988 Apr;7(4):913–918. doi: 10.1002/j.1460-2075.1988.tb02896.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  73. Plemper R. K., Böhmler S., Bordallo J., Sommer T., Wolf D. H. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature. 1997 Aug 28;388(6645):891–895. doi: 10.1038/42276. [DOI] [PubMed] [Google Scholar]
  74. Pueyo J. J., Chrispeels M. J., Herman E. M. Degradation of transport-competent destabilized phaseolin with a signal for retention in the endoplasmic reticulum occurs in the vacuole. Planta. 1995;196(3):586–596. doi: 10.1007/BF00203660. [DOI] [PubMed] [Google Scholar]
  75. Rubin R., Levanony H., Galili G. Evidence for the presence of two different types of protein bodies in wheat endosperm. Plant Physiol. 1992 Jun;99(2):718–724. doi: 10.1104/pp.99.2.718. [DOI] [PMC free article] [PubMed] [Google Scholar]
  76. Sanderfoot A. A., Raikhel N. V. The specificity of vesicle trafficking: coat proteins and SNAREs. Plant Cell. 1999 Apr;11(4):629–642. doi: 10.1105/tpc.11.4.629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. Shimoni Y., Galili G. Intramolecular disulfide bonds between conserved cysteines in wheat gliadins control their deposition into protein bodies. J Biol Chem. 1996 Aug 2;271(31):18869–18874. doi: 10.1074/jbc.271.31.18869. [DOI] [PubMed] [Google Scholar]
  78. Shusta E. V., Raines R. T., Plückthun A., Wittrup K. D. Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments. Nat Biotechnol. 1998 Aug;16(8):773–777. doi: 10.1038/nbt0898-773. [DOI] [PubMed] [Google Scholar]
  79. Skowronek M. H., Hendershot L. M., Haas I. G. The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP. Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1574–1578. doi: 10.1073/pnas.95.4.1574. [DOI] [PMC free article] [PubMed] [Google Scholar]
  80. Staehelin L. A. The plant ER: a dynamic organelle composed of a large number of discrete functional domains. Plant J. 1997 Jun;11(6):1151–1165. doi: 10.1046/j.1365-313x.1997.11061151.x. [DOI] [PubMed] [Google Scholar]
  81. Sze H, Li X, Palmgren MG. Energization of plant cell membranes by H+-pumping ATPases. Regulation and biosynthesis . Plant Cell. 1999 Apr;11(4):677–690. doi: 10.1105/tpc.11.4.677. [DOI] [PMC free article] [PubMed] [Google Scholar]
  82. Tatu U., Helenius A. Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J Cell Biol. 1997 Feb 10;136(3):555–565. doi: 10.1083/jcb.136.3.555. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Townsley F. M., Wilson D. W., Pelham H. R. Mutational analysis of the human KDEL receptor: distinct structural requirements for Golgi retention, ligand binding and retrograde transport. EMBO J. 1993 Jul;12(7):2821–2829. doi: 10.1002/j.1460-2075.1993.tb05943.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Valls L. A., Hunter C. P., Rothman J. H., Stevens T. H. Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide. Cell. 1987 Mar 13;48(5):887–897. doi: 10.1016/0092-8674(87)90085-7. [DOI] [PubMed] [Google Scholar]
  85. Vitale A., Bielli A., Ceriotti A. The Binding Protein Associates with Monomeric Phaseolin. Plant Physiol. 1995 Apr;107(4):1411–1418. doi: 10.1104/pp.107.4.1411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  86. Wieland F. T., Gleason M. L., Serafini T. A., Rothman J. E. The rate of bulk flow from the endoplasmic reticulum to the cell surface. Cell. 1987 Jul 17;50(2):289–300. doi: 10.1016/0092-8674(87)90224-8. [DOI] [PubMed] [Google Scholar]
  87. Wiertz E. J., Jones T. R., Sun L., Bogyo M., Geuze H. J., Ploegh H. L. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell. 1996 Mar 8;84(5):769–779. doi: 10.1016/s0092-8674(00)81054-5. [DOI] [PubMed] [Google Scholar]
  88. Wiertz E. J., Tortorella D., Bogyo M., Yu J., Mothes W., Jones T. R., Rapoport T. A., Ploegh H. L. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature. 1996 Dec 5;384(6608):432–438. doi: 10.1038/384432a0. [DOI] [PubMed] [Google Scholar]
  89. Wolins N., Bosshart H., Küster H., Bonifacino J. S. Aggregation as a determinant of protein fate in post-Golgi compartments: role of the luminal domain of furin in lysosomal targeting. J Cell Biol. 1997 Dec 29;139(7):1735–1745. doi: 10.1083/jcb.139.7.1735. [DOI] [PMC free article] [PubMed] [Google Scholar]
  90. d'Enfert C., Gensse M., Gaillardin C. Fission yeast and a plant have functional homologues of the Sar1 and Sec12 proteins involved in ER to Golgi traffic in budding yeast. EMBO J. 1992 Nov;11(11):4205–4211. doi: 10.1002/j.1460-2075.1992.tb05514.x. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Plant Cell are provided here courtesy of Oxford University Press

RESOURCES