Direct interaction between BKCa potassium channel and microtubule-associated protein 1A

被引:32
作者
Park, SM
Liu, GX
Kubal, A
Fury, M
Cao, LX
Marx, SO [1 ]
机构
[1] Columbia Univ Coll Phys & Surg, Dept Med, Div Cardiol, New York, NY USA
[2] Columbia Univ Coll Phys & Surg, Dept Med, Ctr Mol Cardiol, New York, NY USA
[3] Columbia Univ Coll Phys & Surg, Dept Pharmacol, New York, NY USA
[4] Columbia Univ Coll Phys & Surg, Dept Physiol & Cellular Biophys, New York, NY USA
来源
FEBS LETTERS | 2004年 / 570卷 / 1-3期
基金
美国国家卫生研究院;
关键词
BKCa; potassium channel; cytoskeleton; microtubule associated protein; macromolecular complex;
D O I
10.1016/j.febslet.2004.06.037
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The BKCa channel, a potassium channel that is allosterically activated by voltage and calcium, is expressed in both excitable and non-excitable cells. The channel plays an important role in regulating membrane excitability. The channel activity can be modulated by post-translational modifications such as phosphorylation. Recently, hippocampal BKCa channels were shown to be directly modulated by assembly/disassembly of the submembranous actin cytoskeleton. Here, we report that the BKCa channel physically interacts with the light chain of microtubule associated protein 1A (MAP1A). The light chain was isolated in a yeast two-hybrid screen of a human brain cDNA library. The specificity of the interaction was demonstrated in biochemical experiments utilizing GST fusion protein pulldown assays and reciprocal co-immunoprecipitations from rat brain. Furthermore, utilizing immunofluorescence, the BKCa channel and MAP1A co-localize in the Purkinje cell layer of the cerebellum. These studies identify a novel interaction between the C-terminal tail of the BKCa channel and the light chain of MAP1A, which enables channel association with and modulation by the cytoskeleton. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:143 / 148
页数:6
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