期刊
COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY
卷 14, 期 12, 页码 -出版社
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/cshperspect.a041247
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资金
- Wellcome [202642/Z/16/Z]
- European Research Council Consolidator grant [817708]
- Biotechnology and Biological Sciences Research Council (BBSRC) grant
- European Research Council (ERC) [817708] Funding Source: European Research Council (ERC)
- Wellcome Trust [202642/Z/16/Z] Funding Source: Wellcome Trust
ERAD is a quality control mechanism mediated by ubiquitin-ligase complexes, which targets misfolded, unassembled, or mislocalized proteins in the endoplasmic reticulum for degradation in the cytosolic proteasome. ERAD also regulates the degradation of a subset of folded proteins, influencing critical ER functions.
Misfolded, potentially toxic proteins in the lumen and membrane of the endoplasmic reticulum (ER) are eliminated by proteasomes in the cytosol through ER-associated degradation (ERAD). The ERAD process involves the recognition of substrates in the lumen and membrane of the ER, their translocation into the cytosol, ubiquitination, and delivery to the proteasome for degradation. These ERAD steps are performed by membrane-embedded ubiquitin-ligase complexes of different specificity that together cover a wide range of substrates. Besides misfolded proteins, ERAD further contributes to quality control by targeting unassembled and mislocalized proteins. ERAD also targets a restricted set of folded proteins to influence critical ER functions such as sterol biosynthesis, calcium homeostasis, or ER contacts with other organelles. This review describes the ubiquitin-ligase complexes and the principles guiding protein degradation by ERAD.
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