Apoptosis Initiated When BH3 Ligands Engage Multiple Bcl-2 Homologs, Not Bax or Bak

Author:

Willis Simon N.12,Fletcher Jamie I.12,Kaufmann Thomas12,van Delft Mark F.12,Chen Lin12,Czabotar Peter E.12,Ierino Helen12,Lee Erinna F.12,Fairlie W. Douglas12,Bouillet Philippe12,Strasser Andreas12,Kluck Ruth M.12,Adams Jerry M.12,Huang David C. S.12

Affiliation:

1. The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3050, Australia.

2. Department of Medical Biology, University of Melbourne, Parkville, Victoria 3010, Australia.

Abstract

A central issue in the regulation of apoptosis by the Bcl-2 family is whether its BH3-only members initiate apoptosis by directly binding to the essential cell-death mediators Bax and Bak, or whether they can act indirectly, by engaging their pro-survival Bcl-2–like relatives. Contrary to the direct-activation model, we show that Bax and Bak can mediate apoptosis without discernable association with the putative BH3-only activators (Bim, Bid, and Puma), even in cells with no Bim or Bid and reduced Puma. Our results indicate that BH3-only proteins induce apoptosis at least primarily by engaging the multiple pro-survival relatives guarding Bax and Bak.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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