Das, Tanuza Shin, Sang Chul Song, Eun Joo Kim, Eunice EunKyeong 2024-01-19T17:31:44Z 2024-01-19T17:31:44Z 2021-09-05 2020-06 1661-6596 https://pubs.kist.re.kr/handle/201004/118574 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. English MDPI TUMOR-SUPPRESSOR UBIQUITIN DYNAMICS PROTEIN STABILITY DOWN-REGULATION PHOSPHORYLATION ACTIVATION USP4 LOCALIZATION SUMOYLATION MECHANISMS Regulation of Deubiquitinating Enzymes by Post-Translational Modifications Article 10.3390/ijms21114028 1 INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.21, no.11 INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 21 11 scie scopus 000543400300290 2-s2.0-85086044696 Biochemistry & Molecular Biology Chemistry, Multidisciplinary Biochemistry & Molecular Biology Chemistry Review 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