VCP and PSMF1: antagonistic regulators of proteasome activity
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Author(s)
Clemen, Christoph S
Marko, Marija
Strucksberg, Karl-Heinz
Behrens, Juliane
Wittig, Ilka
Gaertner, Linda
Winter, Lilli
Chevessier, Frederic
Matthias, Jan
Tuerk, Matthias
Tangavelou, Karthikeyan
Schuetz, Johanna
Arhzaouy, Khalid
Klopffleisch, Karsten
Hanisch, Franz-Georg
Rottbauer, Wolfgang
Bluemcke, Ingmar
Just, Steffen
Eichinger, Ludwig
Hofmann, Andreas
Schroeder, Rolf
Griffith University Author(s)
Year published
2015
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Show full item recordAbstract
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 ...
View more >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.
View less >
View more >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.
View less >
Journal Title
Biochemical and Biophysical Research Communications
Volume
463
Copyright Statement
© 2015, Elsevier. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (http://creativecommons.org/licenses/by-nc-nd/4.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, providing that the work is properly cited.
Subject
Medicinal and biomolecular chemistry
Biochemistry and cell biology
Medical biochemistry and metabolomics
Medical parasitology