A first line of defense against ER stress

Journal of Cell Biology

Volumn 198, Issue 3, 2012, Pages 277-279

  Pincus, David ^a   Walter, Peter ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; GLUCOSE REGULATED PROTEIN 78; HYDROLASE; TRANSFERASE;

ADENOSINE DIPHOSPHATE RIBOSYLATION; ARTICLE; CRYSTAL STRUCTURE; ENDOPLASMIC RETICULUM STRESS; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN PROCESSING; SIGNAL TRANSDUCTION; UNFOLDED PROTEIN RESPONSE;

ADENOSINE DIPHOSPHATE; ANIMALS; ENDOPLASMIC RETICULUM; HEAT-SHOCK PROTEINS; HUMANS; PROTEINS;

EID: 84866438777     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201207076     Document Type: Article

References (12)

1. Bukau, B., J. Weissman, and A. Horwich. 2006. Molecular chaperones and protein quality control. Cell. 125:443-451. http://dx.doi.org/10.1016/j.cell.2006.04.014
2. Carlsson, L., and E. Lazarides. 1983. ADP-ribosylation of the Mr 83,000 stress-inducible and glucose-regulated protein in avian and mammalian cells: Modulation by heat shock and glucose starvation. Proc. Natl. Acad. Sci. USA. 80:4664-4668. http://dx.doi.org/10.1073/pnas.80.15.4664
3. Chambers, J.E., K. Petrova, G. Tomba, M. Vendruscolo, and D. Ron. 2012. ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load. J. Cell Biol. 198: 371-385.
4. Dorner, A.J., L.C. Wasley, and R.J. Kaufman. 1992. Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells. EMBO J. 11:1563-1571.
5. Gülow, K., D. Bienert, and I.G. Haas. 2002. BiP is feed-back regulated by control of protein translation efficiency. J. Cell Sci. 115:2443-2452.
6. Hendershot, L.M., J. Ting, and A.S. Lee. 1988. Identity of the immunoglobulin heavy-chain-binding protein with the 78,000-dalton glucose-regulated protein and the role of posttranslational modifications in its binding function. Mol. Cell. Biol. 8:4250-4256.
7. Ledford, B.E., and D.F. Jacobs. 1986. Translational control of ADP-ribosylation in eucaryotic cells. Eur. J. Biochem. 161:661-667. http://dx.doi.org/10.1111/j.1432-1033.1986.tb10491.x
8. Leno, G.H., and B.E. Ledford. 1989. ADP-ribosylation of the 78-kDa glucose-regulated protein during nutritional stress. Eur. J. Biochem. 186:205-211. http://dx.doi.org/10.1111/j.1432-1033.1989.tb15196.x
9. Otero, J.H., B. Lizák, and L.M. Hendershot. 2010. Life and death of a BiP substrate. Semin. Cell Dev. Biol. 21:472-478. http://dx.doi.org/10.1016/j.semcdb.2009.12.008
10. Schlecht, R., A.H. Erbse, B. Bukau, and M.P. Mayer. 2011. Mechanics of Hsp70 chaperones enables differential interaction with client proteins. Nat. Struct. Mol. Biol. 18:345-351. http://dx.doi.org/10.1038/nsmb.2006
11. Sitia, R., and I. Braakman. 2003. Quality control in the endoplasmic reticulum protein factory. Nature. 426:891-894. http://dx.doi.org/10.1038/nature02262
12. Walter, P., and D. Ron. 2011. The unfolded protein response: From stress pathway to homeostatic regulation. Science. 334:1081-1086. http://dx.doi.org/10.1126/science.1209038