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

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
Description
Summary: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.
ISSN:2041-1723

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