Putting the brakes on the unfolded protein response

Journal of Cell Biology

Volumn 193, Issue 1, 2011, Pages 17-19

  Sicheri, Frank ^a   Silverman, Robert H ^b  

^a MOUNT SINAI HOSPITAL   (Canada)

^b LERNER RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN IRE1;

ENDOPLASMIC RETICULUM STRESS; ENZYME ACTIVITY; HUMAN; MOLECULAR MECHANICS; NOTE; PRIORITY JOURNAL; PROTEIN DOMAIN; UNFOLDED PROTEIN RESPONSE;

EIF-2 KINASE; ENDOPLASMIC RETICULUM; HUMANS; PROTEIN FOLDING; UNFOLDED PROTEIN RESPONSE;

EID: 79955501953     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.201101105     Document Type: Note

References (17)

1. Bernales, S., K.L. McDonald, and P. Walter. 2006. Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol. 4:e423. doi:10.1371/journal.pbio.0040423.
2. Chawla, A., S. Chakrabarti, G. Ghosh, and M. Niwa. 2011. Attenuation of yeast UPR is essential for survival and is mediated by Ire1 kinase. J. Cell Biol. 193:41-50.
3. Cox, J.S., and P. Walter. 1996. A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell. 87:391-404. doi:10.1016/S0092-8674(00)81360-4.
4. Cox, J.S., C.E. Shamu, and P. Walter. 1993. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell. 73:1197-1206. doi:10.1016/0092-8674(93)90648-A.
5. Dong, B., and R.H. Silverman. 1999. Alternative function of a protein kinase homology domain in 2', 5'-oligoadenylate dependent RNase L. Nucleic Acids Res. 27:439-445. doi:10.1093/nar/27.2.439.
6. Dong, B., M. Niwa, P. Walter, and R.H. Silverman. 2001. Basis for regulated RNA cleavage by functional analysis of RNase L and Ire1p. RNA. 7:361-373. doi:10.1017/S1355838201002230.
7. Lee, K.P., M. Dey, D. Neculai, C. Cao, T.E. Dever, and F. Sicheri. 2008. Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing. Cell. 132:89-100. doi:10.1016/j.cell.2007.10.057.
8. Marciniak, S.J., and D. Ron. 2006. Endoplasmic reticulum stress signaling in disease. Physiol. Rev. 86:1133-1149. doi:10.1152/physrev.00015.2006.
9. Mori, K., W. Ma, M.J. Gething, and J. Sambrook. 1993. A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell. 74:743-756. doi:10.1016/0092-8674(93)90521-Q.
10. Nolen, B., S. Taylor, and G. Ghosh. 2004. Regulation of protein kinases; controlling activity through activation segment conformation. Mol. Cell. 15:661-675. doi:10.1016/j.molcel.2004.08.024.
11. Papa, F.R., C. Zhang, K. Shokat, and P. Walter. 2003. Bypassing a kinase activity with an ATP-competitive drug. Science. 302:1533-1537. doi:10.1126/science.1090031.
12. Rubio, C.A., D. Pincus, A. Korennykh, S. Schuck, H. El-Samad, and P. Walter. 2011. Homeostaic adaptation to endoplasmic reticulum stress depends on Ire1 kinase activity. J. Cell Biol. 193:171-184.
13. Schuck, S., W.A. Prinz, K.S. Thorn, C. Voss, and P. Walter. 2009. Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response. J. Cell Biol. 187:525-536. doi:10.1083/jcb.200907074.
14. Shamu, C.E., and P. Walter. 1996. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15:3028-3039.
15. Sidrauski, C., and P. Walter. 1997. The transmembrane kinase Ire1p is a sitespecific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell. 90:1031-1039. doi:10.1016/S0092-8674(00)80369-4.
16. Travers, K.J., C.K. Patil, L. Wodicka, D.J. Lockhart, J.S. Weissman, and P. Walter. 2000. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell. 101:249-258. doi:10.1016/S0092-8674(00)80835-1.
17. Zhou, A., B.A. Hassel, and R.H. Silverman. 1993. Expression cloning of 2-5Adependent RNAase: a uniquely regulated mediator of interferon action. Cell. 72:753-765. doi:10.1016/0092-8674(93)90403-D.