Journal
TRAFFIC
Volume 9, Issue 6, Pages 861-870Publisher
WILEY
DOI: 10.1111/j.1600-0854.2008.00729.x
Keywords
degradation; ER; glycosylation; molecular chaperone; proteasome; proteolysis; transport; ubiquitin
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Funding
- NCRR NIH HHS [P41 RR006009-13S10160] Funding Source: Medline
- NHLBI NIH HHS [HL58541, R01 HL058541] Funding Source: Medline
- NIGMS NIH HHS [R01 GM075061, R01 GM075061-02, GM075061] Funding Source: Medline
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Secretory and membrane proteins that fail to fold in the endoplasmic reticulum (ER) are retained and may be sorted for ER-associated degradation (ERAD). During ERAD, ER-associated components such as molecular chaperones and lectins recognize folding intermediates and specific oligosaccharyl modifications on ERAD substrates. Substrates selected for ERAD are then targeted for ubiquitin- and proteasome-mediated degradation. Because the catalytic steps of the ubiquitin-proteasome system reside in the cytoplasm, soluble ERAD substrates that reside in the ER lumen must be retrotranslocated back to the cytoplasm prior to degradation. In contrast, it has been less clear how polytopic, integral membrane substrates are delivered to enzymes required for ubiquitin conjugation and to the proteasome. In this review, we discuss recent studies addressing how ERAD substrates are recognized, ubiquitinated and delivered to the proteasome and then survey current views of how soluble and integral membrane substrates may be retrotranslocated.
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