Cleaning up in the endoplasmic reticulum: ubiquitin in charge
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/nsmb.2793.pdf
Reference131 articles.
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3. Ron, D. & Walter, P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8, 519–529 (2007).
4. Needham, P.G. & Brodsky, J.L. How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: the early history of ERAD. Biochim. Biophys. Acta 1833, 2447–2457 (2013).
5. Lippincott-Schwartz, J., Bonifacino, J.S., Yuan, L.C. & Klausner, R.D. Degradation from the endoplasmic reticulum: disposing of newly synthesized proteins. Cell 54, 209–220 (1988).Refs. 5 and 6 were the first to demonstrate that unassembled endogenous membrane proteins are rapidly degraded after import into the ER, thus defining a new pathway of protein degradation at the ER.
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