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Mechanisms of caspase activation

Journal

CURRENT OPINION IN CELL BIOLOGY
Volume 15, Issue 6, Pages 725-731

Publisher

CURRENT BIOLOGY LTD
DOI: 10.1016/j.ceb.2003.10.009

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Funding

  1. NCI NIH HHS [CA69381] Funding Source: Medline
  2. NHLBI NIH HHS [HL51399] Funding Source: Medline

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The core effectors of apoptosis encompass proteolytic enzymes of the caspase family, which reside as latent precursors in most nucleated metazoan cells. A majority of studies on apoptosis are based on the assumption that caspase precursors are activated by cleavage, a common mechanism for most protease zymogen activations. Although this appears to be true for the executioner caspases, recent research points to a distinct activation mechanism for the initiator caspases that trigger the apoptotic pathways. This mechanism is proximity-induced dimerization without cleavage, and its elucidation has led to the revision of concepts of feedback regulation of apoptosis.

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