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Published online 5 February 2001. doi:10.1083/jcb.152.3.483
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© The Rockefeller University Press, 0021-9525/2001//483 $5.00
The Journal of Cell Biology, Volume 152, Number 3, , 2001 483-490

Original Article

Diablo Promotes Apoptosis by Removing Miha/Xiap from Processed Caspase 9



Paul G. Ekerta,b, John Silkea, Christine J. Hawkinsc, Anne M. Verhagena, and David L. Vauxa

a The Walter and Eliza Hall Institute, The Royal Melbourne Hospital, Victoria 3050, Australia
b Murdoch Children's Research Institute, Royal Children's Hospital, Parkville 3052, Australia
c Department of Haematology and Oncology, Royal Children's Hospital, Parkville 3052, Australia
The Walter & Eliza Hall Institute of Medical Research, Post Office, The Royal Melbourne Hospital, Victoria 3050, Australia.61-3-9347-085261-3-9345-2544

vaux{at}wehi.edu.au

MIHA is an inhibitor of apoptosis protein (IAP) that can inhibit cell death by direct interaction with caspases, the effector proteases of apoptosis. DIABLO is a mammalian protein that can bind to IAPs and antagonize their antiapoptotic effect, a function analogous to that of the proapoptotic Drosophila molecules, Grim, Reaper, and HID. Here, we show that after UV radiation, MIHA prevented apoptosis by inhibiting caspase 9 and caspase 3 activation. Unlike Bcl-2, MIHA functioned after release of cytochrome c and DIABLO from the mitochondria and was able to bind to both processed caspase 9 and processed caspase 3 to prevent feedback activation of their zymogen forms. Once released into the cytosol, DIABLO bound to MIHA and disrupted its association with processed caspase 9, thereby allowing caspase 9 to activate caspase 3, resulting in apoptosis.

Key Words: apoptosis • IAPs • DIABLO • caspases • BIR

© 2001 The Rockefeller University Press

Abbreviations used in this paper: BIR, baculoviral IAP repeat; CARD, caspase recruitment domain; IAP, inhibitor of apoptosis protein; PI, propidium iodide.


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