Origin and Functional Evolution of the Cdc48/p97/VCP AAA+ Protein Unfolding and Remodeling Machine
Name
nihms742308.pdf
Size
577.24 KB
Format
Adobe PDF
Checksum (MD5)
1e1b433ab96e5385633bf882a0224c80
Author(s)
Barthelme, Dominik
Sauer, Robert T.
Date Issued
December 2015
Journal
Journal of Molecular Biology
Publisher
Elsevier
Citation
Barthelme, Dominik and Robert T. Sauer. “Origin and Functional Evolution of the Cdc48/p97/VCP AAA+ Protein Unfolding and Remodeling Machine.” Journal of Molecular Biology 428, 9 (May 2016): 1861–1869 © 2015 Elsevier Ltd
Version
Author's final manuscript
Abstract
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. Keywords: AAA + machine; protein remodeling; human disease
MIT Department
Massachusetts Institute of Technology. Department of Biology
Terms of Use
Creative Commons Attribution-NonCommercial-NoDerivs License
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1016/J.JMB.2015.11.015
