Caspase activation, inhibition, and reactivation: a mechanistic view

Protein Sci. 2004 Aug;13(8):1979-87. doi: 10.1110/ps.04789804.


Caspases, a unique family of cysteine proteases, execute programmed cell death (apoptosis). Caspases exist as inactive zymogens in cells and undergo a cascade of catalytic activation at the onset of apoptosis. The activated caspases are subject to inhibition by the inhibitor-of-apoptosis (IAP) family of proteins. This inhibition can be effectively removed by diverse proteins that share an IAP-binding tetrapeptide motif. Recent structural and biochemical studies have revealed the underlying molecular mechanisms for these processes in mammals and in Drosophila. This paper reviews these latest advances.

Publication types

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

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Apoptosis / physiology*
  • Caspases / chemistry*
  • Caspases / metabolism*
  • Drosophila / metabolism
  • Enzyme Activation / physiology
  • Enzyme Reactivators / metabolism
  • Humans
  • Inhibitor of Apoptosis Proteins
  • Mammals / metabolism
  • Protein Structure, Tertiary
  • Proteins / chemistry*
  • Proteins / metabolism*


  • Enzyme Reactivators
  • Inhibitor of Apoptosis Proteins
  • Proteins
  • Caspases