Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2009 Mar 27;284(13):8223-7.
doi: 10.1074/jbc.R800050200. Epub 2008 Nov 13.

SUMOylation and De-SUMOylation: Wrestling With Life's Processes

Affiliations
Free PMC article
Review

SUMOylation and De-SUMOylation: Wrestling With Life's Processes

Edward T H Yeh. J Biol Chem. .
Free PMC article

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.

Figures

FIGURE 1.
FIGURE 1.
SUMOylation and de-SUMOylation. SUMOylation is a dynamic process that is mediated by activating (E1), conjugating (E2), and ligating (E3) enzymes and readily reversed by the SENP family in human. SUMOylation and de-SUMOylation regulate a diverse spectrum of biological responses, from transcription, cell division, and signal transduction to carcinogenesis and viral replication.

Similar articles

See all similar articles

Cited by 185 articles

See all "Cited by" articles

MeSH terms

LinkOut - more resources

Feedback