Direct addition of BimL to mitochondria does not lead to cytochrome c release
- Author(s)
- Terradillos, O; Montessuit, S; Huang, DCS; Martinou, JC;
- Details
- Publication Year 2002-07-03,Volume 522,Issue #1-3,Page 29-34
- Journal Title
- FEBS LETTERS
- Publication Type
- Journal Article
- Abstract
- Pro-apoptotic members of the Bcl-2 family can be subdivided in two classes according to their structure: a group including Bax, Bak, and Bok that display Bcl-2 homology (BH) 1, BH2 and BH3 domains and a second group including Bid (BH3 interacting domain death agonist), Bad, Bim (Bcl-2 interacting mediator of cell death) and several others that contain only a BH3 domain, the BH3-only proteins. The BH3-only proteins have been proposed to activate pro-apoptotic members of the Bax subfamily to trigger a mitochondrial pathway that leads to the release of cytochrome c and other apoptogenic factors. Here we report that the mechanism of action of Bim is different from that of Bid. Although overexpression of Bid or Bim in cells leads to cytochrome c release, only Bid is able to trigger the release of cytochrome c through Bax activation when added directly to isolated mitochondria. Bim(L), although unable to activate Bax, can directly inhibit Bcl-2 or Bcl-X-L. Our data suggest two functional classes of BH3-only proteins: those such as Bid which directly activate Bax-like proteins leading to mitochondrial membrane permeability and apoptosis and those such as Bim which inhibit anti-apoptotic proteins and render the cells more susceptible to apoptogenic stimuli. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- BCL-X-L; BH3 DOMAIN; FAMILY MEMBER; MOTOR COMPLEX; CELL-DEATH; APOPTOSIS; BAX; SURVIVAL; PHOSPHORYLATION; EXPRESSION
- Publisher's Version
- https://doi.org/10.1016/S0014-5793(02)02871-5
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2002-07-03 12:00:00