SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting.

MS Rodriguez, C Dargemont, Ronald Thomas Hay

Research output: Contribution to journalArticlepeer-review

578 Citations (Scopus)

Abstract

SUMO-1 is a small ubiquitin-related modifier that is covalently linked to many cellular protein targets. Proteins modified by SUMO-1 and the SUMO-l-activating and -conjugating enzymes are located predominantly in the nucleus. Here we define a transferable sequence containing the psi KXE motif, where psi represents a large hydrophobic amino acid, that confers the ability to be SUMO-l-modified on proteins to which it is linked. Whereas addition of short sequences from p53 and I kappaB alpha containing the psi KXE motif, to a carrier protein is sufficient for modification in vitro, modification in vivo requires the additional presence of a nuclear localization signal. Thus, protein substrates must be targeted to the nucleus to undergo SUMO-1 conjugation.

Original languageEnglish
Pages (from-to)12654-12659
Number of pages6
JournalJournal of Biological Chemistry
Volume276
Publication statusPublished - 20 Apr 2001

Keywords

  • GTPASE-ACTIVATING PROTEIN
  • NF-KAPPA-B
  • UBIQUITIN-RELATED MODIFIER
  • PORE COMPLEX
  • COVALENT MODIFICATION
  • ENZYME
  • PML
  • LOCALIZATION
  • DEGRADATION
  • RANGAP1

Fingerprint

Dive into the research topics of 'SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting.'. Together they form a unique fingerprint.

Cite this