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ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together
Author(s): Brodsky JL, McCracken AA
Source: TRENDS IN CELL BIOLOGY    Volume: 7    Issue: 4    Pages: 151-156    Published: APR 1997  
Times Cited: 168     References: 44     
Abstract: A protein-degradation pathway associated with the endoplasmic reticulum (ER) can selectively remove polypeptides from the secretory pathway. The mechanisms of this ER-associated protein degradation were obscure, but recent studies using both yeast and mammalian cells have indicated that substrates for degradation are targeted to the cytosol where proteolysis is catalysed by the proteasome. The degradation process is now known to comprise at least three distinct events: first, recognition of a polypeptide for degradation; second, efflux of this substrate from the ER to the cytosol; and, finally, degradation by the proteasome. This review summarizes recent advances in understanding how each of these steps is achieved.
Document Type: Article
Language: English
Reprint Address: Brodsky, JL (reprint author), UNIV PITTSBURGH, DEPT BIOL SCI, PITTSBURGH, PA 15260 USA
Addresses:
1. UNIV NEVADA, DEPT BIOL, RENO, NV 89557 USA
Publisher: ELSEVIER SCI LTD, THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD, OXON, ENGLAND OX5 1GB
Subject Category: Cell Biology
IDS Number: WP270
ISSN: 0962-8924
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