A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of α-actinin-2

被引:55
作者
Cukovic, D
Lu, GWK
Wible, B
Steele, DF
Fedida, D
机构
[1] Univ British Columbia, Dept Physiol, Vancouver, BC V6T 1Z3, Canada
[2] Case Western Reserve Univ, Metrohlth Med Ctr, Rammelkamp Ctr Res, Cleveland, OH 44106 USA
基金
加拿大健康研究院; 美国国家卫生研究院;
关键词
potassium channel; Kv1.5; actinin-2; cytoskeleton;
D O I
10.1016/S0014-5793(01)02505-4
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 interaction between the amino terminus of Kv1-type potassium channels and alpha -actinin-2 has been investigated. Using a combination of yeast two-hybrid analysis and in vitro binding assays, alpha -actinin-2 was found to bind to the N-termini of both Kv1.4 and Kv1.5 but not to the equivalent segments of Kv1.1, Kv1.2 or Kv1.3, Deletion analysis in the in vitro binding assays delineated the actinin binding region of Kv1.5 to between amino acids 73 and 148 of the channel. The Kv1.5 binding sites in alpha -actinin-2 were found to lie within actinin's internal spectrin repeats. Unlike the reported interaction between actinin and the NMDA receptor, calmodulin was found to have no effect on actinin binding to Kv1.5. (C) 2001 Published by Elsevier Science B.V, on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:87 / 92
页数:6
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