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

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.

Bibliographic Details
Main Authors:	Liang Chen, Guixin Zhu, Eleanor M. Johns, Xiaolu Yang
Format:	Article
Language:	English
Published:	Nature Publishing Group 2018-03-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-018-03499-z

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spelling	doaj-eb78696545ab4e1d9c7dde25e577469b2021-05-11T09:38:45ZengNature Publishing GroupNature Communications2041-17232018-03-019111410.1038/s41467-018-03499-zTRIM11 activates the proteasome and promotes overall protein degradation by regulating USP14Liang Chen0Guixin Zhu1Eleanor M. Johns2Xiaolu Yang3Department of Cancer Biology and Abramson Family Cancer Research Institute, Perelman School of Medicine, University of PennsylvaniaDepartment of Cancer Biology and Abramson Family Cancer Research Institute, Perelman School of Medicine, University of PennsylvaniaDepartment of Cancer Biology and Abramson Family Cancer Research Institute, Perelman School of Medicine, University of PennsylvaniaDepartment of Cancer Biology and Abramson Family Cancer Research Institute, Perelman School of Medicine, University of PennsylvaniaThe 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.https://doi.org/10.1038/s41467-018-03499-z
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Liang Chen Guixin Zhu Eleanor M. Johns Xiaolu Yang
spellingShingle	Liang Chen Guixin Zhu Eleanor M. Johns Xiaolu Yang TRIM11 activates the proteasome and promotes overall protein degradation by regulating USP14 Nature Communications
author_facet	Liang Chen Guixin Zhu Eleanor M. Johns Xiaolu Yang
author_sort	Liang Chen
title	TRIM11 activates the proteasome and promotes overall protein degradation by regulating USP14
title_short	TRIM11 activates the proteasome and promotes overall protein degradation by regulating USP14
title_full	TRIM11 activates the proteasome and promotes overall protein degradation by regulating USP14
title_fullStr	TRIM11 activates the proteasome and promotes overall protein degradation by regulating USP14
title_full_unstemmed	TRIM11 activates the proteasome and promotes overall protein degradation by regulating USP14
title_sort	trim11 activates the proteasome and promotes overall protein degradation by regulating usp14
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2018-03-01
description	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.
url	https://doi.org/10.1038/s41467-018-03499-z
work_keys_str_mv	AT liangchen trim11activatestheproteasomeandpromotesoverallproteindegradationbyregulatingusp14 AT guixinzhu trim11activatestheproteasomeandpromotesoverallproteindegradationbyregulatingusp14 AT eleanormjohns trim11activatestheproteasomeandpromotesoverallproteindegradationbyregulatingusp14 AT xiaoluyang trim11activatestheproteasomeandpromotesoverallproteindegradationbyregulatingusp14
_version_	1721449589761900544

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

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