DIABLO Promotes Apoptosis by Removing MIHA/XIAP from Processed Caspase 9

doi:10.1083/jcb.152.3.483

Published online 29 January 2001. doi:10.1083/jcb.152.3.483

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© The Rockefeller University Press, 0021-9525/2001/2/483/ $5.00
The Journal of Cell Biology, Volume 152, Number 3, February 5, 2001 483-490

Original Article

DIABLO Promotes Apoptosis by Removing MIHA/XIAP from Processed Caspase 9

Paul G. Ekert^a,b, John Silke^a, Christine J. Hawkins^c, Anne M. Verhagen^a, and David L. Vaux^a
^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

Correspondence to: David L. Vaux, The Walter & Eliza Hall Institute of Medical Research, Post Office, The Royal Melbourne Hospital, Victoria 3050, Australia. Tel:61-3-9345-2544 Fax:61-3-9347-0852 E-mail:vaux{at}wehi.edu.au.

MIHA is an inhibitor of apoptosis protein (IAP) that can inhibitcell death by direct interaction with caspases, the effectorproteases of apoptosis. DIABLO is a mammalian protein that canbind to IAPs and antagonize their antiapoptotic effect, a functionanalogous 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 caspase3 activation. Unlike Bcl-2, MIHA functioned after release ofcytochrome c and DIABLO from the mitochondria and was able tobind to both processed caspase 9 and processed caspase 3 toprevent feedback activation of their zymogen forms. Once releasedinto the cytosol, DIABLO bound to MIHA and disrupted its associationwith processed caspase 9, thereby allowing caspase 9 to activatecaspase 3, resulting in apoptosis.

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

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