Journal article
VCP and PSMF1: Antagonistic regulators of proteasome activity
Christoph S Clemen, Marija Marko, Karl-Heinz Strucksberg, Juliane Behrens, Ilka Wittig, Linda Gaertner, Lilli Winter, Frederic Chevessier, Jan Matthias, Matthias Tuerk, Karthikeyan Tangavelou, Johanna Schuetz, Khalid Arhzaouy, Karsten Klopffleisch, Franz-Georg Hanisch, Wolfgang Rottbauer, Ingmar Bluemcke, Steffen Just, Ludwig Eichinger, Andreas Hofmann Show all
Biochemical and Biophysical Research Communications | ACADEMIC PRESS INC ELSEVIER SCIENCE | Published : 2015
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.
Grants
Awarded by German Research Foundation (DFG)
Awarded by Fritz-Thyssen-Foundation
Awarded by Australian Research Council (ARC)
Funding Acknowledgements
Grant support by the German Research Foundation (DFG) within the framework of the multi-location research group FOR1228 (grants CL 381/3-2 to CSC, HA 2092/23-2 to FGH, RO 2173/4-2 to WR, JU 2859/1-2 to SJ, EI 399/7-2 to LE, and SCHR 562/9-2 to RS), within the collaborative research consortium 815 (project Z1 to IW), and for individual research projects (grants CL 381/1-1 to CSC and SCHR 562/7-1 to RS), by the Fritz-Thyssen-Foundation (grant 10.07.1.165 to RS and CSC), the Australian Research Council (ARC) (grant LE120100071 to AH), by Koln Fortune (to CSC and LE), and by the Interdisciplinary Center for Clinical Research (IZKF) of the Clinical Center Erlangen (to MT) is gratefully acknowledged.