Regulation of Deubiquitinating Enzymes by Post-Translational Modifications

Authors
Das, TanuzaShin, Sang ChulSong, Eun JooKim, Eunice EunKyeong
Issue Date
2020-06
Publisher
MDPI
Citation
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.21, no.11
Abstract
Ubiquitination and deubiquitination play a critical role in all aspects of cellular processes, and the enzymes involved are tightly regulated by multiple factors including posttranslational modifications like most other proteins. Dysfunction or misregulation of these enzymes could have dramatic physiological consequences, sometimes leading to diseases. Therefore, it is important to have a clear understanding of these regulatory processes. Here, we have reviewed the posttranslational modifications of deubiquitinating enzymes and their consequences on the catalytic activity, stability, abundance, localization, and interaction with the partner proteins.
Keywords
TUMOR-SUPPRESSOR; UBIQUITIN DYNAMICS; PROTEIN STABILITY; DOWN-REGULATION; PHOSPHORYLATION; ACTIVATION; USP4; LOCALIZATION; SUMOYLATION; MECHANISMS; TUMOR-SUPPRESSOR; UBIQUITIN DYNAMICS; PROTEIN STABILITY; DOWN-REGULATION; PHOSPHORYLATION; ACTIVATION; USP4; LOCALIZATION; SUMOYLATION; MECHANISMS; post-translational modification (PTM); deubiquitinase (DUB); deubiquitinating enzyme; activity; localization; interaction; disease
ISSN
1661-6596
URI
https://pubs.kist.re.kr/handle/201004/118574
DOI
10.3390/ijms21114028
Appears in Collections:
KIST Article > 2020
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