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c-Jun氨基末端激酶-3对纯化的线粒体电压依赖性阴离子通道的磷酸化作用改变了通道的电压依赖性。

Phosphorylation of purified mitochondrial Voltage-Dependent Anion Channel by c-Jun N-terminal Kinase-3 modifies channel voltage-dependence.

作者信息

Gupta Rajeev, Ghosh Subhendu

机构信息

Department of Physiology, All India Institute of Medical Sciences, New Delhi, India.

Department of Biophysics, University of Delhi South Campus, India.

出版信息

Biochim Open. 2017 Mar 10;4:78-87. doi: 10.1016/j.biopen.2017.03.002. eCollection 2017 Jun.

Abstract

Voltage-Dependent Anion Channel (VDAC) phosphorylated by c-Jun N-terminal Kinase-3 (JNK3) was incorporated into the bilayer lipid membrane. Single-channel electrophysiological properties of the native and the phosphorylated VDAC were compared. The open probability versus voltage curve of the native VDAC displayed symmetry around the voltage axis, whereas that of the phosphorylated VDAC showed asymmetry. This result indicates that phosphorylation by JNK3 modifies voltage-dependence of VDAC.

摘要

被c-Jun氨基末端激酶3(JNK3)磷酸化的电压依赖性阴离子通道(VDAC)被整合到双层脂质膜中。比较了天然VDAC和磷酸化VDAC的单通道电生理特性。天然VDAC的开放概率与电压曲线在电压轴周围呈对称分布,而磷酸化VDAC的则呈不对称分布。这一结果表明JNK3介导的磷酸化改变了VDAC的电压依赖性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7818/5802065/c2ba6eb72a94/gr1.jpg

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