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In this issue |
Members of the Bcl-2 family regulate developmentally programmed cell death
and stress-induced apoptosis. The anti-apoptotic members (e.g. Bcl-2) possess
3/4 characteristic BH domains (BH1-BH4). Of the pro-apoptotic members, some
possess 2/3 BH domains (e.g. Bax and Bak); the remainder have only the BH3
domain (e.g. Bad and Bim). In a Commentary on
p. 1567, Phillippe Bouillet
and Andreas Strasser discuss the roles of such `BH3-only' proteins in
apoptosis. Apoptotic stimuli regulate the transcription, activity and
subcellular localization of BH3-only proteins, and the existence of multiple
members of this subfamily appears to allow cells to respond to stresses as
diverse as loss of attachment and 
-radiation. The proteins function by
binding to and inhibiting anti-apoptotic Bcl-2-family members, preventing them
from blocking pathways that lead to activation of the apoptotic effectors
caspases. This mode of action appears to be distinct from that of the multi-BH
pro-apoptotic members (which may disrupt mitochondrial integrity).
Nevertheless, BH3-only and multi-BH pro-apoptotic proteins are mutually
dependent, and both are essential for stress-induced apoptosis.
Related articles in JCS:
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