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

Rajeev Gupta; Subhendu Ghosh

doi:10.1016/j.biopen.2017.03.002

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

Rajeev Gupta, Subhendu Ghosh

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

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.

Original language	English
Pages (from-to)	78-87
Number of pages	10
Journal	Biochimie Open
Volume	4
DOIs	https://doi.org/10.1016/j.biopen.2017.03.002
State	Published - 1 Jun 2017
Externally published	Yes

Keywords

Bilayer electrophysiology
Phosphorylation
Voltage-Dependent Anion Channel
c-Jun N-terminal Kinase-3

ASJC Scopus subject areas

Biochemistry

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10.1016/j.biopen.2017.03.002

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

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.",

keywords = "Bilayer electrophysiology, Phosphorylation, Voltage-Dependent Anion Channel, c-Jun N-terminal Kinase-3",

author = "Rajeev Gupta and Subhendu Ghosh",

note = "Publisher Copyright: {\textcopyright} 2017 The Author(s)",

year = "2017",

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doi = "10.1016/j.biopen.2017.03.002",

language = "English",

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TY - JOUR

T1 - Phosphorylation of purified mitochondrial Voltage-Dependent Anion Channel by c-Jun N-terminal Kinase-3 modifies channel voltage-dependence

AU - Gupta, Rajeev

AU - Ghosh, Subhendu

PY - 2017/6/1

Y1 - 2017/6/1

N2 - 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.

AB - 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.

KW - Bilayer electrophysiology

KW - Phosphorylation

KW - Voltage-Dependent Anion Channel

KW - c-Jun N-terminal Kinase-3

UR - http://www.scopus.com/inward/record.url?scp=85016395798&partnerID=8YFLogxK

U2 - 10.1016/j.biopen.2017.03.002

DO - 10.1016/j.biopen.2017.03.002

M3 - Article

AN - SCOPUS:85016395798

SN - 2214-0085

VL - 4

SP - 78

EP - 87

JO - Biochimie Open

JF - Biochimie Open

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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