Structure and function of the AAA + ATPase p97/Cdc48p

被引：129
|
作者：
Xia, Di [1 ]
Tang, Wai Kwan [1 ]
Ye, Yihong [2 ]
机构：
[1] NCI, Cell Biol Lab, Ctr Canc Res, NIH, Bldg 37, Bethesda, MD 20892 USA
[2] NIDDK, Mol Biol Lab, NIH, Bethesda, MD 20892 USA
来源：
GENE | 2016年 / 583卷 / 01期
基金：
美国国家卫生研究院;
关键词：
p97/CDC48; AAA plus ATPase; Segregase; Unfoldase; Protein quality control; ER-associated degradation; Chromatin-associated degradation; Mitochondria-associated degradation; Ribosome-associated degradation; Membrane fusion; Ubiquitin; Proteasome; INCLUSION-BODY MYOPATHY; ENDOPLASMIC-RETICULUM; ATPASE ACTIVITY; CONFORMATIONAL-CHANGES; MEMBRANE-PROTEIN; QUALITY-CONTROL; PAGET-DISEASE; P97; ADAPTER; N-DOMAIN; TRANSCRIPTION FACTOR;
D O I：
10.1016/j.gene.2016.02.042
中图分类号：
Q3 [遗传学];
学科分类号：
071007 ; 090102 ;
摘要：
p97 (also known as valosin-containing protein (VCP) in mammals or Cdc48p in Saccharomyces cerevisiae) is an evolutionarily conserved ATPase present in all eukaryotes and archaebacteria. In conjunction with a collection of cofactors and adaptors, p97/Cdc48p performs an array of biological functions mostly through modulating the stability of 'client' proteins. Using energy from ATP hydrolysis, p97/Cdc48p segregates these molecules from immobile cellular structures such as protein assemblies, membrane organelles, and chromatin. Consequently, the released polypeptides can be efficiently degraded by the ubiquitin proteasome system or recycled. This review summarizes our current understanding of the structure and function of this essential cellular chaperoning system. Published by Elsevier B.V.
引用
收藏
页码：64 / 77
页数：14
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