ER stress response: Getting the UPR hand on misfolded proteins

Current Biology

Volumn 10, Issue 14, 2000, Pages

  Hampton, Randolph Y ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0034644111     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(00)00583-2     Document Type: Review

References (29)

1. 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. 101:2000;249-258.
2. Ng D., Spear E.D., Walter P. The unfolded protein response regulates multiple aspects of secetory and membrane protein biogenesis and ER quality control. J Cell Biol. 2000;. in press.
3. Casagrande R., Stern P., Diehn M., Shamu C., Osario M., Zúñiga M., Brown P.O., Ploegh H. Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway. Mol Cell. 5:2000;729-735.
4. Pahl H.L. Signal transduction from the endoplasmic reticulum to the cell nucleus. Physiol Rev. 79:1999;683-701.
5. Kozutsumi Y., Segal M., Normington K., Gething M.J., Sambrook J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature. 332:1988;462-464.
6. Rose M.D., Misra L.M., Vogel J.P. KAR2, a karyogamy gene. is the yeast homolog of the mammalian BiP/GRP78 gene Cell. 57:1989;1211-1221.
7. Normington K., Kohno K., Kozutsumi Y., Gething M.J., Sambrook J. S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell. 57:1989;1223-1236.
8. Cox J.S., Shamu C.E., Walter P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell. 73:1993;1197-1206.
9. Cox J.S., Walter P. A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell. 87:1996;391-404.
10. +/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell. 74:1993;743-756.
11. Sidrauski C., Walter P. The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell. 90:1997;1031-1039.
12. Sidrauski C., Cox J.S., Walter P. tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Cell. 87:1996;405-413.
13. Sidrauski C., Chapman R., Walter P. The unfolded protein response: an intracellular signalling pathway with many surprising features. Trends Cell Biol. 8:1998;245-249.
14. Shamu C.E. Splicing: HACking into the unfolded-protein response. Curr Biol. 8:1998;R121-R123.
15. Shamu C.E., Walter P. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15:1996;3028-3039.
16. Bertolotti A., Zhang Y., Hendershot L.M., Harding H.P., Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded protein response. Nat Cell Biol. 2:2000;326-332.
17. Tirasophon W., Welihinda A.A., Kaufman R.J. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev. 12:1998;1812-1824.
18. Niwa M., Sidrauski C., Kaufman R.J., Walter P. A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response. Cell. 99:1999;691-702.
19. Harding H.P., Zhang Y., Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature. 397:1999;271-274.
20. Harding H.P., Zhang Y., Bertolotti A., Zeng H., Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell. 5:2000;897-904.
21. Nikawa J., Yamashita S. IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae. Mol Microbiol. 6:1992;1441-1446.
22. Cox J.S., Chapman R.E., Walter P. The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane. Mol Biol Cell. 8:1997;1805-1814.
23. Wodicka L., Dong H., Mittmann M., Ho M.H., Lockhart D.J. Genome-wide expression monitoring in Saccharomyces cerevisiae. Nat Biotechnol. 15:1997;1359-1367.
24. Hampton R.Y., Gardner R.G., Rine J. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol Biol Cell. 7:1996;2029-2044.
25. Hampton R.Y., Bhakta H. Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase. Proc Natl Acad Sci USA. 94:1997;12944-12948.
26. Knop M., Finger A., Braun T., Hellmuth K., Wolf D.H. Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J. 15:1996;753-763.
27. Bonifacino J.S., Weissman A.M. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu Rev Cell Dev Biol. 14:1998;19-57.
28. Brodsky J.L., McCracken A.A. ER protein quality control and proteasome-mediated protein degradation. Semin Cell Dev Biol. 10:1999;507-513.
29. Zhou M., Schekman R. The engagement of Sec61p in the ER dislocation process. Mol Cell. 4:1999;925-934.