A SIM-ultaneous role for SUMO and ubiquitin

J. Jefferson P. Perry, John A. Tainer, Michael N. Boddy

Research output: Contribution to journalReview articlepeer-review

187 Scopus citations

Abstract

Ubiquitin and ubiquitin-like proteins (Ubls) share a β-GRASP fold and have key roles in cellular growth and suppression of genome instability. Despite their common fold, SUMO and ubiquitin are classically portrayed as distinct, and they can have antagonistic roles. Recently, a new family of proteins, the small ubiquitin-related modifier (SUMO)-targeted ubiquitin ligases (STUbLs), which directly connect sumoylation and ubiquitylation, has been discovered. Uniquely, STUbLs use SUMO-interaction motifs (SIMs) to recognize their sumoylated targets. STUbLs are global regulators of protein sumoylation levels, and cells lacking STUbLs display genomic instability and hypersensitivity to genotoxic stress. The human STUbL, RNF4, is implicated in several diseases including cancer, highlighting the importance of characterizing the cellular functions of STUbLs.

Original languageEnglish (US)
Pages (from-to)201-208
Number of pages8
JournalTrends in Biochemical Sciences
Volume33
Issue number5
DOIs
StatePublished - May 2008
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Fingerprint

Dive into the research topics of 'A SIM-ultaneous role for SUMO and ubiquitin'. Together they form a unique fingerprint.

Cite this