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| ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together |
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| 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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| |  |  |  |  | | | | Record from Web of Science® | |  |  | | | | | | |