Skip to main content
American Journal of Human Genetics logoLink to American Journal of Human Genetics
. 1997 Aug;61(2):267–272. doi: 10.1086/514865

The final stage of gene expression: chaperones and the regulation of protein fate.

J Ashkenas 1, P H Byers 1
PMCID: PMC1715893  PMID: 9311729

Full text

PDF
269

Selected References

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

  1. Bush K. T., Goldberg A. L., Nigam S. K. Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J Biol Chem. 1997 Apr 4;272(14):9086–9092. doi: 10.1074/jbc.272.14.9086. [DOI] [PubMed] [Google Scholar]
  2. Cheng S. H., Gregory R. J., Marshall J., Paul S., Souza D. W., White G. A., O'Riordan C. R., Smith A. E. Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell. 1990 Nov 16;63(4):827–834. doi: 10.1016/0092-8674(90)90148-8. [DOI] [PubMed] [Google Scholar]
  3. Chessler S. D., Byers P. H. Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern. J Biol Chem. 1992 Apr 15;267(11):7751–7757. [PubMed] [Google Scholar]
  4. Chessler S. D., Wallis G. A., Byers P. H. Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta. J Biol Chem. 1993 Aug 25;268(24):18218–18225. [PubMed] [Google Scholar]
  5. Cox J. S., Walter P. A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell. 1996 Nov 1;87(3):391–404. doi: 10.1016/s0092-8674(00)81360-4. [DOI] [PubMed] [Google Scholar]
  6. Farr G. W., Scharl E. C., Schumacher R. J., Sondek S., Horwich A. L. Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms. Cell. 1997 Jun 13;89(6):927–937. doi: 10.1016/s0092-8674(00)80278-0. [DOI] [PubMed] [Google Scholar]
  7. Finley D., Chau V. Ubiquitination. Annu Rev Cell Biol. 1991;7:25–69. doi: 10.1146/annurev.cb.07.110191.000325. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. Hayes S. A., Dice J. F. Roles of molecular chaperones in protein degradation. J Cell Biol. 1996 Feb;132(3):255–258. doi: 10.1083/jcb.132.3.255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hebert D. N., Foellmer B., Helenius A. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell. 1995 May 5;81(3):425–433. doi: 10.1016/0092-8674(95)90395-x. [DOI] [PubMed] [Google Scholar]
  11. Hebert D. N., Simons J. F., Peterson J. R., Helenius A. Calnexin, calreticulin, and Bip/Kar2p in protein folding. Cold Spring Harb Symp Quant Biol. 1995;60:405–415. doi: 10.1101/sqb.1995.060.01.045. [DOI] [PubMed] [Google Scholar]
  12. 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]
  13. Jensen T. J., Loo M. A., Pind S., Williams D. B., Goldberg A. L., Riordan J. R. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell. 1995 Oct 6;83(1):129–135. doi: 10.1016/0092-8674(95)90241-4. [DOI] [PubMed] [Google Scholar]
  14. Kim P. S., Arvan P. Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J Cell Biol. 1995 Jan;128(1-2):29–38. doi: 10.1083/jcb.128.1.29. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kopito R. R. ER quality control: the cytoplasmic connection. Cell. 1997 Feb 21;88(4):427–430. doi: 10.1016/s0092-8674(00)81881-4. [DOI] [PubMed] [Google Scholar]
  16. Kuznetsov G., Bush K. T., Zhang P. L., Nigam S. K. Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia. Proc Natl Acad Sci U S A. 1996 Aug 6;93(16):8584–8589. doi: 10.1073/pnas.93.16.8584. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Kuznetsov G., Chen L. B., Nigam S. K. Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum. J Biol Chem. 1997 Jan 31;272(5):3057–3063. doi: 10.1074/jbc.272.5.3057. [DOI] [PubMed] [Google Scholar]
  18. Lamandé S. R., Chessler S. D., Golub S. B., Byers P. H., Chan D., Cole W. G., Sillence D. O., Bateman J. F. Endoplasmic reticulum-mediated quality control of type I collagen production by cells from osteogenesis imperfecta patients with mutations in the pro alpha 1 (I) chain carboxyl-terminal propeptide which impair subunit assembly. J Biol Chem. 1995 Apr 14;270(15):8642–8649. doi: 10.1074/jbc.270.15.8642. [DOI] [PubMed] [Google Scholar]
  19. Leppä S., Sistonen L. Heat shock response--pathophysiological implications. Ann Med. 1997 Feb;29(1):73–78. doi: 10.3109/07853899708998745. [DOI] [PubMed] [Google Scholar]
  20. Maquat L. E. Defects in RNA splicing and the consequence of shortened translational reading frames. Am J Hum Genet. 1996 Aug;59(2):279–286. [PMC free article] [PubMed] [Google Scholar]
  21. Nagata K. Hsp47: a collagen-specific molecular chaperone. Trends Biochem Sci. 1996 Jan;21(1):22–26. doi: 10.1016/0968-0004(96)80881-4. [DOI] [PubMed] [Google Scholar]
  22. Ou W. J., Cameron P. H., Thomas D. Y., Bergeron J. J. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature. 1993 Aug 26;364(6440):771–776. doi: 10.1038/364771a0. [DOI] [PubMed] [Google Scholar]
  23. Parsell D. A., Kowal A. S., Singer M. A., Lindquist S. Protein disaggregation mediated by heat-shock protein Hsp104. Nature. 1994 Dec 1;372(6505):475–478. doi: 10.1038/372475a0. [DOI] [PubMed] [Google Scholar]
  24. Pasyk E. A., Foskett J. K. Mutant (delta F508) cystic fibrosis transmembrane conductance regulator Cl- channel is functional when retained in endoplasmic reticulum of mammalian cells. J Biol Chem. 1995 May 26;270(21):12347–12350. doi: 10.1074/jbc.270.21.12347. [DOI] [PubMed] [Google Scholar]
  25. Qu D., Teckman J. H., Omura S., Perlmutter D. H. Degradation of a mutant secretory protein, alpha1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J Biol Chem. 1996 Sep 13;271(37):22791–22795. doi: 10.1074/jbc.271.37.22791. [DOI] [PubMed] [Google Scholar]
  26. Rapoport T. A., Rolls M. M., Jungnickel B. Approaching the mechanism of protein transport across the ER membrane. Curr Opin Cell Biol. 1996 Aug;8(4):499–504. doi: 10.1016/s0955-0674(96)80027-5. [DOI] [PubMed] [Google Scholar]
  27. Rechsteiner M., Rogers S. W. PEST sequences and regulation by proteolysis. Trends Biochem Sci. 1996 Jul;21(7):267–271. [PubMed] [Google Scholar]
  28. Saris N., Holkeri H., Craven R. A., Stirling C. J., Makarow M. The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates. J Cell Biol. 1997 May 19;137(4):813–824. doi: 10.1083/jcb.137.4.813. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Sidrauski C., Cox J. S., Walter P. tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Cell. 1996 Nov 1;87(3):405–413. doi: 10.1016/s0092-8674(00)81361-6. [DOI] [PubMed] [Google Scholar]
  30. Smith L. T., Schwarze U., Goldstein J., Byers P. H. Mutations in the COL3A1 gene result in the Ehlers-Danlos syndrome type IV and alterations in the size and distribution of the major collagen fibrils of the dermis. J Invest Dermatol. 1997 Mar;108(3):241–247. doi: 10.1111/1523-1747.ep12286441. [DOI] [PubMed] [Google Scholar]
  31. Teckman J. H., Perlmutter D. H. The endoplasmic reticulum degradation pathway for mutant secretory proteins alpha1-antitrypsin Z and S is distinct from that for an unassembled membrane protein. J Biol Chem. 1996 May 31;271(22):13215–13220. doi: 10.1074/jbc.271.22.13215. [DOI] [PubMed] [Google Scholar]
  32. Teckman J. H., Qu D., Perlmutter D. H. Molecular pathogenesis of liver disease in alpha1-antitrypsin deficiency. Hepatology. 1996 Dec;24(6):1504–1516. doi: 10.1002/hep.510240635. [DOI] [PubMed] [Google Scholar]
  33. Varshavsky A. The N-end rule. Cell. 1992 May 29;69(5):725–735. doi: 10.1016/0092-8674(92)90285-k. [DOI] [PubMed] [Google Scholar]
  34. Wang Y., Schnegelsberg P. N., Dausman J., Jaenisch R. Functional redundancy of the muscle-specific transcription factors Myf5 and myogenin. Nature. 1996 Feb 29;379(6568):823–825. doi: 10.1038/379823a0. [DOI] [PubMed] [Google Scholar]
  35. Ward C. L., Omura S., Kopito R. R. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell. 1995 Oct 6;83(1):121–127. doi: 10.1016/0092-8674(95)90240-6. [DOI] [PubMed] [Google Scholar]
  36. Ware F. E., Vassilakos A., Peterson P. A., Jackson M. R., Lehrman M. A., Williams D. B. The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J Biol Chem. 1995 Mar 3;270(9):4697–4704. doi: 10.1074/jbc.270.9.4697. [DOI] [PubMed] [Google Scholar]
  37. Welihinda A. A., Tirasophon W., Green S. R., Kaufman R. J. Gene induction in response to unfolded protein in the endoplasmic reticulum is mediated through Ire1p kinase interaction with a transcriptional coactivator complex containing Ada5p. Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4289–4294. doi: 10.1073/pnas.94.9.4289. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Wu Y., Whitman I., Molmenti E., Moore K., Hippenmeyer P., Perlmutter D. H. A lag in intracellular degradation of mutant alpha 1-antitrypsin correlates with the liver disease phenotype in homozygous PiZZ alpha 1-antitrypsin deficiency. Proc Natl Acad Sci U S A. 1994 Sep 13;91(19):9014–9018. doi: 10.1073/pnas.91.19.9014. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from American Journal of Human Genetics are provided here courtesy of American Society of Human Genetics

RESOURCES