期刊
CELL DEATH AND DIFFERENTIATION
卷 16, 期 8, 页码 1075-1082出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/cdd.2009.61
关键词
tBid/Bax; mitochondria; TOM complex; apoptosis
资金
- Swedish Research Council
- Swedish and the Stockholm Cancer Societies
- Swedish Childhood Cancer Foundation
- EC FP-6 (Oncodeath and Chemores)
- Wenner-Gren Foundation, Stockholm, Sweden
The release of pro-apoptotic proteins from the mitochondria is a key event in cell death signaling that is regulated by Bcl-2 family proteins. For example, cleavage of the BH3-only protein, Bid, by multiple proteases leads to the formation of truncated Bid that, in turn, promotes the insertion/oligomerization of Bax into the mitochondrial outer membrane, resulting in pore formation and the release of proteins residing in the intermembrane space. Bax, a monomeric protein in the cytosol is targeted to the mitochondria by a yet unknown mechanism. Several proteins of the outer mitochondrial membrane have been proposed to act as receptors for Bax, among them the voltage-dependent anion channel, VDAC, and the mitochondrial protein translocase of the outer membrane, the TOM complex. Alternatively, the unique mitochondrial phospholipid, cardiolipin, has been ascribed a similar function. Here, we review recent work on the mechanisms of activation and the targeting of Bax to the mitochondria and discuss the advantages and limitations of the methods used to study this process. Cell Death and Differentiation (2009) 16, 1075-1082; doi:10.1038/cdd.2009.61; published online 12 June 2009
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据