Unknown

Dataset Information

0

SUMOylation and De-SUMOylation: wrestling with life's processes.


ABSTRACT: The small ubiquitin-like modifier (SUMO) is a ubiquitin-like protein that covalently modifies a large number of cellular proteins. SUMO modification has emerged as an important regulatory mechanism for protein function and localization. SUMOylation is a dynamic process that is mediated by activating (E1), conjugating (E2), and ligating (E3) enzymes and readily reversed by a family of ubiquitin-like protein-specific proteases (Ulp) in yeast and sentrin/SUMO-specific proteases (SENP) in human. This review will focus on the de-SUMOylating enzymes with special attention to their biological function.

SUBMITTER: Yeh ET 

PROVIDER: S-EPMC2659178 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

SUMOylation and De-SUMOylation: wrestling with life's processes.

Yeh Edward T H ET  

The Journal of biological chemistry 20081113 13


The small ubiquitin-like modifier (SUMO) is a ubiquitin-like protein that covalently modifies a large number of cellular proteins. SUMO modification has emerged as an important regulatory mechanism for protein function and localization. SUMOylation is a dynamic process that is mediated by activating (E1), conjugating (E2), and ligating (E3) enzymes and readily reversed by a family of ubiquitin-like protein-specific proteases (Ulp) in yeast and sentrin/SUMO-specific proteases (SENP) in human. Thi  ...[more]

Similar Datasets

| S-EPMC1949349 | biostudies-literature
| S-EPMC11301343 | biostudies-literature
| S-EPMC6199952 | biostudies-literature
| S-EPMC8062768 | biostudies-literature
| S-EPMC3697009 | biostudies-literature
| S-EPMC2750016 | biostudies-literature
| S-EPMC4196186 | biostudies-literature
| S-EPMC2572558 | biostudies-literature
| S-EPMC8301837 | biostudies-literature
| S-EPMC8278079 | biostudies-literature