作者: D. Cukovic , G.W-K. Lu , B. Wible , D.F. Steele , D. Fedida
DOI: 10.1016/S0014-5793(01)02505-4
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摘要: Abstract The interaction between the amino terminus of Kv1-type potassium channels and α-actinin-2 has been investigated. Using a combination yeast two-hybrid analysis in vitro binding assays, was found to bind N-termini both Kv1.4 Kv1.5 but not equivalent segments Kv1.1, Kv1.2 or Kv1.3. Deletion assays delineated actinin region acids 73 148 channel. sites were lie within actinin’s internal spectrin repeats. Unlike reported NMDA receptor, calmodulin have no effect on Kv1.5.