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

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...

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Detalles Bibliográficos
Autores principales: Gupta, Rajeev, Ghosh, Subhendu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2017
Materias:
Research paper
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5802065/
https://www.ncbi.nlm.nih.gov/pubmed/29450145
http://dx.doi.org/10.1016/j.biopen.2017.03.002
Descripción
Sumario: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.

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