Insights into a functional model of key deubiquitinases UBP12/13 in plants.
New Phytol
; 242(2): 424-430, 2024 Apr.
Article
en En
| MEDLINE
| ID: mdl-38406992
ABSTRACT
Understanding the complexities of protein ubiquitination is crucial, as it plays a multifaceted role in controlling protein stability, activity, subcellular localization, and interaction, which are central to diverse biological processes. Deubiquitinases (DUBs) serve to reverse ubiquitination, but research progress in plant DUBs is noticeably limited. Among existing studies, UBIQUITIN-SPECIFIC PROTEASE 12 (UBP12) and UBP13 have garnered attention for their extensive role in diverse biological processes in plants. This review systematically summarizes the recent advancements in UBP12/13 studies, emphasizing their function, and their substrate specificity, their relationship with E3 ubiquitin ligases, and the similarities and differences with their mammalian orthologue, USP7. By unraveling the molecular mechanisms of UBP12/13, this review offers in-depth insights into the ubiquitin-proteasome system (UPS) in plants and aims to catalyze further explorations and comprehensive understanding in this field.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Endopeptidasas
/
Complejo de la Endopetidasa Proteasomal
Límite:
Animals
Idioma:
En
Revista:
New Phytol
Asunto de la revista:
BOTANICA
Año:
2024
Tipo del documento:
Article
País de afiliación:
China