FEBS Letters | |
Modulation of Kv4.3 current by accessory subunits | |
Tomaselli, Gordon F1  Deschênes, Isabelle1  | |
[1] Department of Medicine, Institute of Molecular Cardiobiology, Division of Cardiology, Johns Hopkins University, 720 N Rutland Avenue, Ross 844, Baltimore, MD 21205, USA | |
关键词: Ion channel; Potassium; Accessory subunit; I to; transient outward potassium current; KChAP; K channel interacting protein; KChIP; Kv channel interacting protein; MiRP; minK related protein; HERG; human ether-a-go-go related gene; | |
DOI : 10.1016/S0014-5793(02)03296-9 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Kv4.3 encodes the pore-forming subunit of the cardiac transient outward potassium current (I to). hKv4.3-encoded current does not fully replicate cardiac I to, suggesting a functionally significant role for accessory subunits. KChIP2 associates with Kv4.3 and modifies hKv4.3-encoded currents but does not replicate native I to. We examined the effect of several ancillary subunits expressed in the heart on hKv4.3-encoded currents. Remarkably, the ancillary subunits Kvβ3, minK, MiRP-1, the Na channel β1 and KChIP2 increased the density and modified the gating of hKv4.3 current. hKv4.3 promiscuously assembles with ancillary subunits in vitro, functionally modifying the encoded currents; however, the physiological significance is uncertain.
【 授权许可】
Unknown
【 预 览 】
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RO201912020312198ZK.pdf | 182KB | download |