期刊
NATURE CELL BIOLOGY
卷 13, 期 10, 页码 1224-U130出版社
NATURE PORTFOLIO
DOI: 10.1038/ncb2330
关键词
-
类别
资金
- NIH [NS064967, NS37402]
Anti-apoptotic Bcl2 family proteins such as Bcl-x(L) protect cells from death by sequestering apoptotic molecules, but also contribute to normal neuronal function. We find in hippocampal neurons that Bcl-x(L) enhances the efficiency of energy metabolism. Our evidence indicates that Bcl-x(L)interacts directly with the beta-subunit of the F1F0 ATP synthase, decreasing an ion leak within the F1F0 ATPase complex and thereby increasing net transport of H+ by F1F0 during F1F0 ATPase activity. By patch clamping submitochondrial vesicles enriched in F1F0 ATP synthase complexes, we find that, in the presence of ATP, pharmacological or genetic inhibition of Bcl-x(L) activity increases the membrane leak conductance. In addition, recombinant Bcl-x(L) protein directly increases the level of ATPase activity of purified synthase complexes, and inhibition of endogenous Bcl-x(L) decreases the level of F1F0 enzymatic activity. Our findings indicate that increased mitochondrial efficiency contributes to the enhanced synaptic efficacy found in Bcl-x(L)-expressing neurons.
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