Conopeptide Vt3.1 preferentially inhibits BK potassium channels containing β4 subunits via electrostatic interactions

Min Li; Shan Chang; Longjin Yang; Jingyi Shi; Kelli McFarland; Xiao Yang; Alyssa Moller; Chunguang Wang; Xiaoqin Zou; Chengwu Chi; Jianmin Cui

doi:10.1074/jbc.M113.535898

Conopeptide Vt3.1 preferentially inhibits BK potassium channels containing β4 subunits via electrostatic interactions

Min Li
, Shan Chang
, Longjin Yang
, Jingyi Shi
, Kelli McFarland
, Xiao Yang
, Alyssa Moller
, Chunguang Wang
, Xiaoqin Zou
, Chengwu Chi
, Jianmin Cui

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

16 Scopus citations

Abstract

Background: BK channel function is differentially modulated by tissue-specific β (β1-4) subunits. Results: Conopeptide Vt3.1 preferentially inhibits neuronal BK channels containing the β4 subunit. Conclusion: Electrostatic interactions between Vt3.1 and the extracellular loop of β4 decrease voltage-dependent activation of the channel. Significance: Vt3.1 is an excellent tool for studying the structure, function, and roles in neurophysiology of BK channels.

Original language	English
Pages (from-to)	4735-4742
Number of pages	8
Journal	Journal of Biological Chemistry
Volume	289
Issue number	8
DOIs	https://doi.org/10.1074/jbc.M113.535898
State	Published - Feb 21 2014

Access to Document

10.1074/jbc.M113.535898

Cite this

@article{6bd959e0d34d46cd9126702f3b8152eb,

title = "Conopeptide Vt3.1 preferentially inhibits BK potassium channels containing β4 subunits via electrostatic interactions",

abstract = "Background: BK channel function is differentially modulated by tissue-specific β (β1-4) subunits. Results: Conopeptide Vt3.1 preferentially inhibits neuronal BK channels containing the β4 subunit. Conclusion: Electrostatic interactions between Vt3.1 and the extracellular loop of β4 decrease voltage-dependent activation of the channel. Significance: Vt3.1 is an excellent tool for studying the structure, function, and roles in neurophysiology of BK channels.",

author = "Min Li and Shan Chang and Longjin Yang and Jingyi Shi and Kelli McFarland and Xiao Yang and Alyssa Moller and Chunguang Wang and Xiaoqin Zou and Chengwu Chi and Jianmin Cui",

year = "2014",

month = feb,

day = "21",

doi = "10.1074/jbc.M113.535898",

language = "English",

volume = "289",

pages = "4735--4742",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

number = "8",

}

TY - JOUR

T1 - Conopeptide Vt3.1 preferentially inhibits BK potassium channels containing β4 subunits via electrostatic interactions

AU - Li, Min

AU - Chang, Shan

AU - Yang, Longjin

AU - Shi, Jingyi

AU - McFarland, Kelli

AU - Yang, Xiao

AU - Moller, Alyssa

AU - Wang, Chunguang

AU - Zou, Xiaoqin

AU - Chi, Chengwu

AU - Cui, Jianmin

PY - 2014/2/21

Y1 - 2014/2/21

N2 - Background: BK channel function is differentially modulated by tissue-specific β (β1-4) subunits. Results: Conopeptide Vt3.1 preferentially inhibits neuronal BK channels containing the β4 subunit. Conclusion: Electrostatic interactions between Vt3.1 and the extracellular loop of β4 decrease voltage-dependent activation of the channel. Significance: Vt3.1 is an excellent tool for studying the structure, function, and roles in neurophysiology of BK channels.

AB - Background: BK channel function is differentially modulated by tissue-specific β (β1-4) subunits. Results: Conopeptide Vt3.1 preferentially inhibits neuronal BK channels containing the β4 subunit. Conclusion: Electrostatic interactions between Vt3.1 and the extracellular loop of β4 decrease voltage-dependent activation of the channel. Significance: Vt3.1 is an excellent tool for studying the structure, function, and roles in neurophysiology of BK channels.

UR - https://www.scopus.com/pages/publications/84894426204

U2 - 10.1074/jbc.M113.535898

DO - 10.1074/jbc.M113.535898

M3 - Article

C2 - 24398688

AN - SCOPUS:84894426204

SN - 0021-9258

VL - 289

SP - 4735

EP - 4742

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 8

ER -

Conopeptide Vt3.1 preferentially inhibits BK potassium channels containing β4 subunits via electrostatic interactions

Abstract

Access to Document

Other files and links

Fingerprint

Cite this