ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together
ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together
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DOI：
10.1016/s0962-8924(97)01020-9
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发表时间：
1997-04-01
影响因子：
19
通讯作者：
McCracken, AA
中科院分区：
文献类型：
--
作者：
Brodsky, JL;McCracken, AA
与内质网（ER）相关的蛋白质降解途径可以选择性地从分泌途径中去除多肽。这种ER相关蛋白降解的机制尚不清楚，但最近使用酵母和哺乳动物细胞的研究表明，降解底物靶向细胞溶质，其中蛋白酶体催化蛋白水解。现在已知降解过程包括至少三个不同的事件：第一，识别用于降解的多肽;第二，该底物从ER流出到胞质溶胶;最后，由蛋白酶体降解。本文综述了最近的进展，了解如何实现这些步骤。
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.