NSF and p97/VCP: similar at first, different at last

被引：67
作者：
Brunger, AT
DeLaBarre, B
机构：
[1] Stanford Univ, Howard Hughes Med Inst, Stanford, CA 94305 USA
[2] Stanford Univ, Dept Mol & Cellular Physiol, Stanford, CA 94305 USA
[3] Stanford Univ, Dept Neurol, Stanford, CA 94305 USA
[4] Stanford Univ, Dept Neurol Sci, Stanford, CA 94305 USA
[5] Stanford Univ, Stanford Synchrotron Radiat Lab, Stanford, CA 94305 USA
来源：
FEBS LETTERS | 2003年 / 555卷 / 01期
关键词：
AAA protein; vesicle fusion; membrane protein extraction; endoplasmic reticulum-associated degradation;
D O I：
10.1016/S0014-5793(03)01107-4
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
N-Ethylmaleimide sensitive factor (NSF) and p97/ valosin-containing protein (VCP) are distantly related members of the ATPases associated with a variety of cellular activities (AAA) family of proteins. While both proteins have been implied in cellular morphology changes involving membrane compartments or vesicles, more recent evidence seems to imply that NSF is primarily involved in the soluble NSF attachment receptor (SNARE)-mediated vesicle fusion by disassembling the SNARE complex whereas p97/VCP is primarily involved in the extraction of membrane proteins. These functional differences are now corroborated by major structural differences based on recent crystallographic and cryo-electron microscopy studies. This review discusses these recent findings. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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收藏
页码：126 / 133
页数：8
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