UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97 (original) (raw)
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.
Article PDF
Similar content being viewed by others
Author information
Authors and Affiliations
- Cell Biology and Biophysics Unit, EMBL Heidelberg, Meyerhofstraße 1, 69117, Heidelberg, Germany
C. Schuberth - Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany
A. Buchberger
Authors
- C. Schuberth
You can also search for this author inPubMed Google Scholar - A. Buchberger
You can also search for this author inPubMed Google Scholar
Corresponding authors
Correspondence toC. Schuberth or A. Buchberger.
Additional information
Received 8 February 2008; received after revision 12 March 2008; accepted 14 March 2008
Rights and permissions
Open Access This is an open access article distributed under the terms of the Creative Commons Attribution Noncommercial License ( https://creativecommons.org/licenses/by-nc/2.0 ), which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
About this article
Cite this article
Schuberth, C., Buchberger, A. UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97.Cell. Mol. Life Sci. 65, 2360–2371 (2008). https://doi.org/10.1007/s00018-008-8072-8
- Published: 26 April 2008
- Issue Date: August 2008
- DOI: https://doi.org/10.1007/s00018-008-8072-8