JCB logo
Avanti Polar Lipids, Inc.
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 5 February 2001. doi:10.1083/jcb.152.3.483
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 351K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ekert, P. G.
Right arrow Articles by Vaux, D. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ekert, P. G.
Right arrow Articles by Vaux, D. L.
Right arrowPubmed/NCBI databases
*Substance via MeSH
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© 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.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?




  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents