Bera A K, Ghosh S, Das S
Department of Biophysics, University of Delhi South Campus, India.
Biochem Biophys Res Commun. 1995 Apr 6;209(1):213-7. doi: 10.1006/bbrc.1995.1491.
The voltage dependent anion channel (VDAC) of the outer membrane of mitochondria is thought to play a role in transport of metabolites including ATP across mitochondrial membrane and modulate mitochondrial functions such as respiration. However, regulation of this anion channel is only poorly understood. In this paper we demonstrate that VDAC purified from rat liver mitochondria can be phosphorylated by the catalytic subunit of cAMP dependent protein kinase (PKA). PKA phosphorylates VDAC linearly up to fifteenfold in sixty minutes. The level of VDAC phosphorylation increases to twofold and sevenfold of control value after ten and thirty minutes of reaction, respectively. Data presented here suggest the possibility that voltage dependent anion channel of the outer membrane of mitochondria may be a target of PKA in vivo.
线粒体外膜的电压依赖性阴离子通道（VDAC）被认为在包括ATP在内的代谢物跨线粒体膜运输中发挥作用，并调节呼吸等线粒体功能。然而，对这种阴离子通道的调节了解甚少。在本文中，我们证明从大鼠肝脏线粒体中纯化的VDAC可被环磷酸腺苷依赖性蛋白激酶（PKA）的催化亚基磷酸化。PKA在60分钟内将VDAC线性磷酸化至15倍。反应10分钟和30分钟后，VDAC的磷酸化水平分别增加至对照值的2倍和7倍。此处提供的数据表明，线粒体外膜的电压依赖性阴离子通道可能是体内PKA的作用靶点。
