A Mighty "Protein Extractor" of the Cell: Structure and Function of the p97/CDC48 ATPase

被引：143
|
作者：
Ye, Yihong [1 ]
Tang, Wai Kwan [2 ]
Zhang, Ting [1 ]
Xia, Di [2 ]
机构：
[1] NIDDK, Mol Biol Lab, NIH, Bethesda, MD 20892 USA
[2] NCI, Cell Biol Lab, Ctr Canc Res, NIH, Bldg 37, Bethesda, MD 20892 USA
来源：
FRONTIERS IN MOLECULAR BIOSCIENCES | 2017年 / 4卷
基金：
美国国家卫生研究院;
关键词：
AAA ATPase; p97/VCP; Cdc48; chaperones; protein denaturation; protein quality control; neurodegenerative diseases; INCLUSION-BODY MYOPATHY; VALOSIN-CONTAINING PROTEIN; P97; AAA-ATPASE; TRANSITIONAL ENDOPLASMIC-RETICULUM; UNSATURATED FATTY-ACIDS; KAPPA-B-ALPHA; QUALITY-CONTROL; CONFORMATIONAL-CHANGES; MEMBRANE-PROTEIN; UBIQUITIN-LIGASE;
D O I：
10.3389/fmolb.2017.00039
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：
p97/VCP (known as Cdc48 in S. cerevisiae or TER94 in Drosophila) is one of the most abundant cytosolic ATPases. It is highly conserved from archaebacteria to eukaryotes. In conjunction with a large number of cofactors and adaptors, it couples ATP hydrolysis to segregation of polypeptides from immobile cellular structures such as protein assemblies, membranes, ribosome, and chromatin. This often results in proteasomal degradation of extracted polypeptides. Given the diversity of p97 substrates, this "segregase" activity has profound influence on cellular physiology ranging from protein homeostasis to DNA lesion sensing, and mutations in p97 have been linked to several human diseases. Here we summarize our current understanding of the structure and function of this important cellular machinery and discuss the relevant clinical implications.
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页数：20
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