The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7

J Biol Chem. 2000 Sep 1;275(35):26661-4. doi: 10.1074/jbc.C000199200.

Abstract

The inhibitor of apoptosis, cIAP2, contains a putative Ring finger motif at the C terminus. Using in vitro ubiquitination assays, we found that the Ring finger of cIAP2 alone possesses intrinsic ubiquitin ligase activity and promotes substrate-independent ubiquitination. It also promotes ubiquitination of caspases 3 and 7 but not caspase-1. The Ring fingers of c-Cbl and Apc11 failed to promote caspase-7 ubiquitination, suggesting that the Ring finger of cIAP2 itself is involved in substrate recognition.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Caspase 3
  • Caspase 7
  • Caspases / metabolism*
  • Inhibitor of Apoptosis Proteins
  • Ligases / chemistry
  • Ligases / metabolism*
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid
  • Ubiquitin-Protein Ligases
  • Ubiquitins / metabolism*
  • Viral Proteins / chemistry
  • Viral Proteins / metabolism*

Substances

  • Inhibitor of Apoptosis Proteins
  • Ubiquitins
  • Viral Proteins
  • inhibitor of apoptosis, Nucleopolyhedrovirus
  • Ubiquitin-Protein Ligases
  • Caspase 3
  • Caspase 7
  • Caspases
  • Ligases