Unknown

Dataset Information

0

Structure and function of the AAA+ ATPase p97/Cdc48p.


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.

SUBMITTER: Xia D 

PROVIDER: S-EPMC4821690 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structure and function of the AAA+ ATPase p97/Cdc48p.

Xia Di D   Tang Wai Kwan WK   Ye Yihong Y  

Gene 20160303 1


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, membr  ...[more]

Similar Datasets

| S-EPMC5559722 | biostudies-literature
| S-EPMC6967774 | biostudies-literature
| S-EPMC391063 | biostudies-literature
| S-EPMC4677369 | biostudies-literature
| S-EPMC4514128 | biostudies-literature
| S-EPMC1456939 | biostudies-literature
| S-EPMC3309748 | biostudies-literature
| S-EPMC6231190 | biostudies-literature
| S-EPMC5447069 | biostudies-literature
| S-EPMC3971404 | biostudies-literature