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

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