TY - JOUR
T1 - Regulation of deubiquitinating enzymes by post-translational modifications
AU - Das, Tanuza
AU - Shin, Sang Chul
AU - Song, Eun Joo
AU - Kim, Eunice Eunkyeong
N1 - Funding Information:
This work was supported by a National Research Foundation of Korea (NRF) grant funded by the Ministry of Science and ICT (2017R1A2B3007224 and 2019R1A2C2004052). Tanuza Das was supported by Korea Research Fellowship Program through the National Research Foundation of Korea funded by the Ministry of Science and ICT (2017HID3A1A02054608).
Publisher Copyright:
© 2020 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2020/6/1
Y1 - 2020/6/1
N2 - 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.
AB - 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.
KW - Activity
KW - Deubiquitinase (DUB)
KW - Deubiquitinating enzyme
KW - Disease
KW - Interaction
KW - Localization
KW - Post-translational modification (PTM)
UR - http://www.scopus.com/inward/record.url?scp=85086044696&partnerID=8YFLogxK
U2 - 10.3390/ijms21114028
DO - 10.3390/ijms21114028
M3 - Review article
C2 - 32512887
AN - SCOPUS:85086044696
SN - 1661-6596
VL - 21
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
IS - 11
M1 - 4028
ER -