Phosphorylation of purified mitochondrial Voltage-Dependent Anion Channel by c-Jun N-terminal Kinase-3 modifies channel voltage-dependence.
Phosphorylation of purified mitochondrial Voltage-Dependent Anion Channel by c-Jun N-terminal Kinase-3 modifies channel voltage-dependence.
复制标题
DOI：
10.1016/j.biopen.2017.03.002
复制
发表时间：
2017-06
期刊：
影响因子：
--
通讯作者：
Ghosh S
中科院分区：
文献类型：
--
作者：
Gupta R;Ghosh S
将c-Jun N-末端激酶-3（JNK 3）磷酸化的电压依赖性阴离子通道（VDAC）掺入双层脂质膜中。比较了天然和磷酸化VDAC的单通道电生理特性。天然VDAC的开放概率-电压曲线显示围绕电压轴对称，而磷酸化VDAC的开放概率-电压曲线显示不对称。该结果表明JNK 3的磷酸化改变了VDAC的电压依赖性。已在体外进行了JNK 3对纯化的VDAC的磷酸化。已经记录了来自天然和磷酸化VDAC的单通道电流。原生VDAC的开路概率与电压曲线是对称的。磷光体-VDAC开路概率是不对称的，即在负电压下被修改。该结果表明JNK 3的磷酸化改变了VDAC的电压依赖性。
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. Phosphorylation of purified VDAC by JNK3 has been carried out in vitro. Single-channel currents from native and phosphorylated VDAC have been recorded. Open probability vs. voltage curve of native VDAC is symmetric. Phospho-VDAC open probability is asymmetric i.e. modified at negative voltages. This result indicates phosphorylation by JNK3 modifies voltage-dependence of VDAC.