Origin and Functional Evolution of the Cdc48/p97/VCP AAA+ Protein Unfolding and Remodeling Machine

被引：57

作者：

Barthelme, Dominik ^{[1
,2
]}

Sauer, Robert T. ^{[1
]}

机构：

[1] MIT, Dept Biol, 77 Massachusetts Ave, Cambridge, MA 02139 USA

[2] Max Planck Inst Infekt Biol, D-10117 Berlin, Germany

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2016年 / 428卷 / 09期

基金：

美国国家卫生研究院;

关键词：

VALOSIN-CONTAINING PROTEIN; ATPASE ACTIVITY; 20S PROTEASOME; DEUBIQUITINATING ENZYME; CONFORMATIONAL-CHANGES; MECHANISTIC INSIGHTS; CRYSTAL-STRUCTURES; MEMBRANE-FUSION; 26S PROTEASOME; PORE RESIDUES;

D O I：

10.1016/j.jmb.2015.11.015

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：

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. (C) 2015 Elsevier Ltd. All rights reserved.

引用

页码：1861 / 1869

页数：9

共 107 条

[1] Valosin-containing protein (VCP) mutations in sporadic amyotrophic lateral sclerosis
Abramzon, Yevgeniya
Johnson, Janel O.
Scholz, Sonja W.
Taylor, J. P.
Brunetti, Maura
Calvo, Andrea
Mandrioli, Jessica
Benatar, Michael
Mora, Gabriele
Restagno, Gabriella
Chio, Adriano
Traynor, Bryan J.
[J]. NEUROBIOLOGY OF AGING, 2012, 33 (09)
[2] Improved Strains and Plasmid Vectors for Conditional Overexpression of His-Tagged Proteins in Haloferax volcanii
Allers, Thorsten
Barak, Shahar
Liddell, Susan
Wardell, Kayleigh
Mevarech, Moshe
[J]. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2010, 76 (06) : 1759 - 1769
[3] ClpXP, an ATP-powered unfolding and protein-degradation machine
Baker, Tania A.
Sauer, Robert T.
[J]. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 2012, 1823 (01): : 15 - 28
[4] An ALS disease mutation in Cdc48/p97 impairs 20S proteasome binding and proteolytic communication
Barthelme, Dominik
Jauregui, Ruben
Sauer, Robert T.
[J]. PROTEIN SCIENCE, 2015, 24 (09) : 1521 - 1527
[5] Architecture and assembly of the archaeal Cdc48•20S proteasome
Barthelme, Dominik
Chen, James Z.
Grabenstatter, Jonathan
Baker, Tania A.
Sauer, Robert T.
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2014, 111 (17) : E1687 - E1694
[6] Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase
Barthelme, Dominik
Sauer, Robert T.
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2013, 110 (09) : 3327 - 3332
[7] Identification of the Cdc48•20S Proteasome as an Ancient AAA+ Proteolytic Machine
Barthelme, Dominik
Sauer, Robert T.
[J]. SCIENCE, 2012, 337 (6096) : 843 - 846
[8] Distinct conformations of the protein complex p97-Ufd1-Npl4 revealed by electron cryomicroscopy
Bebeacua, Cecilia
Foerster, Andreas
McKeown, Ciaran
Meyer, Hemmo H.
Zhang, Xiaodong
Freemont, Paul S.
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2012, 109 (04) : 1098 - 1103
[9] Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA plus unfoldase
Beckwith, Robyn
Estrin, Eric
Worden, Evan J.
Martin, Andreas
[J]. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2013, 20 (10) : 1164 - +
[10] Role of the ubiquitin-selective CDC48UFD1/NPL4 chaperone (segregase) in ERAD of OLE1 and other substrates
Braun, S
Matuschewski, K
Rape, M
Thoms, S
Jentsch, S
[J]. EMBO JOURNAL, 2002, 21 (04) : 615 - 621

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