TRIM11 activates the proteasome and promotes overall protein degradation by regulating USP14

Liang Chen; Guixin Zhu; Eleanor M. Johns; Xiaolu Yang

doi:10.1038/s41467-018-03499-z

Nature Communications (Mar 2018)

TRIM11 activates the proteasome and promotes overall protein degradation by regulating USP14

Liang Chen,
Guixin Zhu,
Eleanor M. Johns,
Xiaolu Yang

Affiliations

Liang Chen: Department of Cancer Biology and Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania
Guixin Zhu: Department of Cancer Biology and Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania
Eleanor M. Johns: Department of Cancer Biology and Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania
Xiaolu Yang: Department of Cancer Biology and Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania

DOI: https://doi.org/10.1038/s41467-018-03499-z
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 14

Abstract

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The proteasome-bound ubiquitinase USP14 plays an important role in determining proteasome activity and substrate specificity. Here the authors show that TRIM11, a member of the mammalian tripartite motif family, regulates USP14 and is an important activator of the proteasome.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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