SP-RING for SUMO: new functions bloom for a ubiquitin-like protein

Cell. 2001 Oct 5;107(1):5-8. doi: 10.1016/s0092-8674(01)00519-0.

Abstract

SUMO is covalently linked to a variety of cellular proteins. Three groups now describe related E3-like factors that enhance transfer of SUMO to specific proteins. This family of factors includes proteins important for chromosome condensation, signal transduction, and ion channel biogenesis.

Publication types

  • Review

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Fungal Proteins / metabolism
  • GTPase-Activating Proteins / metabolism
  • Humans
  • Ligases*
  • Protein Binding
  • Protein Processing, Post-Translational*
  • SUMO-1 Protein / genetics
  • SUMO-1 Protein / metabolism*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins*
  • Ubiquitin-Protein Ligases*

Substances

  • Fungal Proteins
  • GTPase-Activating Proteins
  • RANGAP1 protein, human
  • SUMO-1 Protein
  • Saccharomyces cerevisiae Proteins
  • Siz2 protein, S cerevisiae
  • Ubiquitin-Protein Ligases
  • Ligases
  • Siz1 protein, S cerevisiae