| Literature DB >> 26945625 |
Di Xia1, Wai Kwan Tang2, Yihong Ye3.
Abstract
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.Entities:
Keywords: AAA+ ATPase; Chromatin-associated degradation; ER-associated degradation; Membrane fusion; Mitochondria-associated degradation; Proteasome; Protein quality control; Ribosome-associated degradation; Segregase; Ubiquitin; Unfoldase; p97/CDC48
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Year: 2016 PMID: 26945625 PMCID: PMC4821690 DOI: 10.1016/j.gene.2016.02.042
Source DB: PubMed Journal: Gene ISSN: 0378-1119 Impact factor: 3.688