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Biochem Biophys Res Commun. 2015 Aug 7;463(4):1210-7. doi: 10.1016/j.bbrc.2015.06.086. Epub 2015 Jun 15.

VCP and PSMF1: Antagonistic regulators of proteasome activity.

Author information

1
Institute of Biochemistry I, Medical Faculty, University of Cologne, 50931 Cologne, Germany. Electronic address: christoph.clemen@uni-koeln.de.
2
Institute of Biochemistry I, Medical Faculty, University of Cologne, 50931 Cologne, Germany.
3
Functional Proteomics, SFB815 Core Unit, Medical Faculty, Goethe University, 60590 Frankfurt, Germany.
4
Molecular Cardiology, Department of Internal Medicine II, University Hospital Ulm, 89081 Ulm, Germany.
5
Institute of Neuropathology, University Hospital Erlangen, 91054 Erlangen, Germany.
6
Department of Neurology, University Hospital Erlangen, 91054 Erlangen, Germany.
7
Institute of Genetics, University of Cologne, 50674 Cologne, Germany.
8
Institute of Biochemistry II, Medical Faculty, and Center for Molecular Medicine Cologne, University of Cologne, 50931 Cologne, Germany.
9
Structural Chemistry Program, Eskitis Institute, Griffith University, Queensland 4111, Australia; Faculty of Veterinary Science, The University of Melbourne, Victoria 3030, Australia.
10
Institute of Neuropathology, University Hospital Erlangen, 91054 Erlangen, Germany. Electronic address: rolf.schroeder@uk-erlangen.de.

Abstract

Protein turnover and quality control by the proteasome is of paramount importance for cell homeostasis. Dysfunction of the proteasome is associated with aging processes and human diseases such as neurodegeneration, cardiomyopathy, and cancer. The regulation, i.e. activation and inhibition of this fundamentally important protein degradation system, is still widely unexplored. We demonstrate here that the evolutionarily highly conserved type II triple-A ATPase VCP and the proteasome inhibitor PSMF1/PI31 interact directly, and antagonistically regulate proteasomal activity. Our data provide novel insights into the regulation of proteasomal activity.

KEYWORDS:

Dictyostelium discoideum; Mouse model; PSMF1; Proteasome; Proteasome inhibitor PI31; Protein quality control; Regulation; Triple-A ATPase; VCP; p97

PMID:
26086101
DOI:
10.1016/j.bbrc.2015.06.086
[Indexed for MEDLINE]
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