Work

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

Year: 2008

Type: review

Abstract: 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.

Source: Cellular and Molecular Life Sciences

DOI: 10.1007/s00018-008-8072-8

Authors: C. Schuberth, A. Buchberger

Institutions: European Molecular Biology Laboratory, Max Planck Society, Max Planck Institute of Biochemistry

Language: English

Topic: Ubiquitin and proteasome pathways

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $4,290

Funder: Deutsche Forschungsgemeinschaft