MITOCHONDRIAL VDAC CAN BE PHOSPHORYLATED BY CYCLIC-AMP-DEPENDENT KINASE

被引：71

作者：

BERA, AK ^{[1
]}

GHOSH, S ^{[1
]}

DAS, S ^{[1
]}

机构：

[1] UNIV DELHI,DEPT BIOPHYS,NEW DELHI 110021,INDIA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 209卷 / 01期

关键词：

D O I：

10.1006/bbrc.1995.1491

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 possibilty that voltage dependent anion channel membrane of mitochondria may be a target of PKA in vivo. (C) 1995 Academic Press,

引用

页码：213 / 217

页数：5

共 10 条

[1] PERMEATION OF HYDROPHILIC SOLUTES THROUGH MITOCHONDRIAL OUTER MEMBRANES - REVIEW ON MITOCHONDRIAL PORINS [J].