Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 21, Issue 11, Pages -Publisher
MDPI
DOI: 10.3390/ijms21114028
Keywords
post-translational modification (PTM); deubiquitinase (DUB); deubiquitinating enzyme; activity; localization; interaction; disease
Funding
- National Research Foundation of Korea (NRF) - Ministry of Science and ICT [2017R1A2B3007224, 2019R1A2C2004052]
- National Research Foundation of Korea - Ministry of Science and ICT [2017HID3A1A02054608]
- National Research Foundation of Korea [2017R1A2B3007224] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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.
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