IAPs, RINGs and Ubiquitylation

Nat Rev Mol Cell Biol. 2005 Apr;6(4):287-97. doi: 10.1038/nrm1621.

Abstract

The inhibitor of apoptosis (IAP) proteins all contain one or more baculoviral IAP repeat motifs, through which they interact with various other proteins. Many IAPs also have another zinc-binding motif, the RING domain, which can recruit E2 ubiquitin-conjugating enzymes and catalyse the transfer of ubiquitin onto target proteins. The number of targets of IAP-mediated ubiquitylation is increasing and recent results indicate that outcomes following ubiquitylation are tantalizingly complex. As well as regulating other proteins, the IAPs themselves are controlled by ubiquitin-mediated degradation.

Publication types

  • Review

MeSH terms

  • Animals
  • Caspases / metabolism
  • Humans
  • Inhibitor of Apoptosis Proteins
  • Protein Structure, Tertiary
  • Proteins / chemistry
  • Proteins / metabolism*
  • Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / metabolism
  • Ubiquitin / metabolism*
  • Ubiquitin-Protein Ligases / metabolism

Substances

  • Inhibitor of Apoptosis Proteins
  • Proteins
  • Tumor Necrosis Factor Receptor-Associated Peptides and Proteins
  • Ubiquitin
  • Ubiquitin-Protein Ligases
  • Caspases