Origin and Functional Evolution of the Cdc48/p97/VCP AAA+ Protein Unfolding and Remodeling Machine

被引：58

作者：

Barthelme, Dominik ^{[1
,2
]}

Sauer, Robert T. ^{[1
]}

机构：

[1] MIT, Dept Biol, 77 Massachusetts Ave, Cambridge, MA 02139 USA

[2] Max Planck Inst Infekt Biol, D-10117 Berlin, Germany

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2016年 / 428卷 / 09期

基金：

美国国家卫生研究院;

关键词：

VALOSIN-CONTAINING PROTEIN; ATPASE ACTIVITY; 20S PROTEASOME; DEUBIQUITINATING ENZYME; CONFORMATIONAL-CHANGES; MECHANISTIC INSIGHTS; CRYSTAL-STRUCTURES; MEMBRANE-FUSION; 26S PROTEASOME; PORE RESIDUES;

D O I：

10.1016/j.jmb.2015.11.015

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：

The AAA+ Cdc48 ATPase (alias p97 or VCP) is a key player in multiple ubiquitin-dependent cell signaling, degradation, and quality control pathways. Central to these broad biological functions is the ability of Cdc48 to interact with a large number of adaptor proteins and to remodel macromolecular proteins and their complexes. Different models have been proposed to explain how Cdc48 might couple ATP hydrolysis to forcible unfolding, dissociation, or remodeling of cellular clients. In this review, we provide an overview of possible mechanisms for substrate unfolding/remodeling by this conserved and essential AAA+ protein machine and their adaption and possible biological function throughout evolution. (C) 2015 Elsevier Ltd. All rights reserved.

引用

页码：1861 / 1869

页数：9

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