Multiple sites of interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2

FEBS Letters

Tucker, Stephen J¹  Jones, Phillippa A¹  Ashcroft, Frances M¹ 

[1] University Laboratory of Physiology, Parks Road, Oxford OX1 3PT, UK

关键词: Inwardly rectifying;    potassium channel;    ATP-sensitive;    Kir6.2;    KATP;   

DOI  :  10.1016/S0014-5793(01)03023-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The amino-terminal and carboxy-terminal domains of inwardly rectifying potassium channel (Kir) subunits are both intracellular. A direct physical interaction between these two domains is involved in the response of Kir channels to regulatory factors such as G-proteins, nucleotides and intracellular pH. We have previously mapped the region within the N-terminal domain of Kir6.2 that interacts with the C-terminus. In this study we use a similar in vitro protein–protein interaction assay to map the regions within the C-terminus which interact with the N-terminus. We find that multiple interaction domains exist within the C-terminus: CID1 (amino acids (aa) 279–323), CID2 (aa 214–222) and CID3 (aa 170–204). These domains correlate with regions previously identified as making important contributions to Kir channel assembly and function. The highly conserved nature of the C-terminus suggests that a similar association with the N-terminus may be a feature common to all members of the Kir family of potassium channels, and that it may be involved in gating of Kir channels by intracellular ligands.

【 授权许可】

Unknown