Conversion of Bcl-2 to a bax-like death effector by caspases

Emily H.Y. Cheng, David G. Kirsch, Rollie J. Clem, Rajani Ravi, Michael B. Kastan, Atul Bedi, Kazuyoshi Ueno, J. Marie Hardwick

Research output: Contribution to journalArticlepeer-review

972 Scopus citations


Caspases are a family of cysteine proteases implicated in the biochemical and morphological changes that occur during apoptosis (programmed cell death). The loop domain of Bcl-2 is cleaved at Asp34 by caspase-3 (CPP32) in vitro, in cells overexpressing caspase-3, and after induction of apoptosis by Fas ligation and interleukin-3 withdrawal. The carboxyl-terminal Bcl-2 cleavage product triggered cell death and accelerated Sindbis virus- induced apoptosis, which was dependent on the BH3 homology and transmembrane domains of Bcl-2. Inhibitor studies indicated that cleavage of Bcl-2 may further activate downstream caspases and contribute to amplification of the caspase cascade. Cleavage-resistant mutants of Bcl-2 had increased protection from interleukin-3 withdrawal and Sindbis virus-induced apoptosis. Thus, cleavage of Bcl-2 by caspases may ensure the inevitability of cell death.

Original languageEnglish (US)
Pages (from-to)1966-1968
Number of pages3
Issue number5345
StatePublished - Dec 12 1997

ASJC Scopus subject areas

  • General


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