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

FEBS Letters - Tập 498 - Trang 87-92 - 2001
D. Cukovic1, G.W-K. Lu1, B. Wible2, D.F. Steele1, D. Fedida1
1Department of Physiology, University of British Columbia, 2146 Health Sciences Mall, Vancouver, BC, Canada V6T 1Z3
2Rammelkamp Center for Research, Metrohealth Medical Center, Case Western Reserve University, Cleveland, OH, USA

Tóm tắt

The interaction between the amino terminus of Kv1‐type potassium channels and α‐actinin‐2 has been investigated. Using a combination of yeast two‐hybrid analysis and in vitro binding assays, α‐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 α‐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.

Tài liệu tham khảo

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FEBS Letters

Tập 498

87-92

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