UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97

被引：227

作者：

Schuberth, C. ^{[1
]}

Buchberger, A. ^{[2
]}

机构：

[1] EMBL Heidelberg, Biol & Biophys Unit, D-69117 Heidelberg, Germany

[2] Max Planck Inst Biochem, Dept Mol Cell Biol, D-82152 Martinsried, Germany

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2008年 / 65卷 / 15期

关键词：

AAA ATPase; valosin-containing protein (VCP); ubiquitin; proteasome system; protein degradation; UBA domain; ubiquitin-like fold;

D O I：

10.1007/s00018-008-8072-8

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 highly conserved AAA ATPase Cdc48/p97 acts on ubiquitylated substrate proteins in cellular processes as diverse as the fusion of homotypic membranes and the degradation of misfolded proteins. The 'Ubiquitin regulatory X' (UBX) domain-containing proteins constitute the so far largest family of Cdc48/p97 cofactors. UBX proteins are involved in substrate recruitment to Cdc48/p97 and in the temporal and spatial regulation of its activity. In combination with UBX-like proteins and other cofactors, they can assemble into a large variety of Cdc48/p97-cofactor complexes possessing distinct cellular functions. This review gives an overview of the different subfamilies of UBX proteins and their functions, and discusses general principles of Cdc48/p97 regulation by these cofactors.

引用

页码：2360 / 2371

页数：12

共 99 条

[91] The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol [J].

Ye, YH ;

Meyer, HH ;

Rapoport, TA .

NATURE, 2001, 414 (6864) :652-656

[92] Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane [J].

Ye, YH ;

Shibata, Y ;

Kikkert, M ;

van Voorden, S ;

Wiertz, E ;

Rapoport, TA .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (40) :14132-14138

[93] A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol [J].

Ye, YH ;

Shibata, Y ;

Yun, C ;

Ron, D ;

Rapoport, TA .

NATURE, 2004, 429 (6994) :841-847

[94] Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97 [J].

Yuan, XM ;

Simpson, P ;

Mckeown, C ;

Kondo, H ;

Uchiyama, K ;

Wallis, R ;

Dreveny, I ;

Keetch, C ;

Zhang, XD ;

Robinson, C ;

Freemont, P ;

Matthews, S .

EMBO JOURNAL, 2004, 23 (07) :1463-1473

[95] Solution structure and interaction surface of the C-terminal domain from p47: A major p97-cofactor involved in SNARE disassembly [J].

Yuan, XM ;

Shaw, A ;

Zhang, XD ;

Kondo, H ;

Lally, J ;

Freemont, PS ;

Matthews, S .

JOURNAL OF MOLECULAR BIOLOGY, 2001, 311 (02) :255-263

[96]

ZHANG SR, 1995, MOL CELL BIOL, V15, P2037

[97] Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation [J].

Zhao, Gang ;

Zhou, Xiaoke ;

Wang, Liqun ;

Li, Guangtao ;

Schindelin, Hermann ;

Lennarz, William J. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (21) :8785-8790

[98] Ataxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates [J].

Zhong, Xiaoyan ;

Pittman, Randall N. .

HUMAN MOLECULAR GENETICS, 2006, 15 (16) :2409-2420

[99] AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation [J].

Zhong, XY ;

Shen, YX ;

Ballar, P ;

Apostolou, A ;

Agami, R ;

Fang, SY .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (44) :45676-45684

← 1 2 3 4 5 6 7 8 9 10 →