Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition

Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2234-8. doi: 10.1073/pnas.93.5.2234.


Three of the predominant features of apoptosis are internucleosomal DNA fragmentation, plasma membrane bleb formation, and retraction of cell processes. We demonstrate that actin is a substrate for the proapoptotic cysteine protease interleukin 1beta-converting enzyme. Actin cleaved by interleukin 1beta-converting enzyme can neither inhibit DNase I nor polymerize to its filamentous form as effectively as intact actin. These findings suggest a mechanism for the coordination of the proteolytic, endonucleolytic, and morphogenetic aspects of apoptosis.

Publication types

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

MeSH terms

  • Actin Cytoskeleton / metabolism
  • Actins / antagonists & inhibitors
  • Actins / metabolism*
  • Animals
  • Apoptosis*
  • Caspase 1
  • Cysteine Endopeptidases / metabolism*
  • Humans
  • Interleukin-1 / metabolism
  • PC12 Cells
  • Peptide Mapping
  • Protein Binding
  • Rats
  • Substrate Specificity


  • Actins
  • Interleukin-1
  • Cysteine Endopeptidases
  • Caspase 1