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XB-ART-20424
FEBS Lett 1994 Dec 19;3562-3:199-203.
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A structural determinant of differential sensitivity of cloned inward rectifier K+ channels to intracellular spermine.

Fakler B , Brändle U , Bond C , Glowatzki E , König C , Adelman JP , Zenner HP , Ruppersberg JP .


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Large subtype-specific differences in the sensitivity of cloned inward-rectifier K+ channels of the IRK1, BIR10 and ROMK1 subtype to being blocked by intracellular spermine (SPM) are described. It is shown, by site-directed mutagenesis, that the four orders of magnitude larger SPM sensitivity of BIR10 channels compared to ROMK1 channels may be explained by a difference in a single amino acid in the putative transmembrane segment TMII. This residue, a negatively charged glutamate in BIR10, is homologous to the residue in IRK1 and ROMK1 which has previously been shown to change gating properties and Mg2+ sensitivity. Differential block by physiological SPM concentrations is suggested as a major functional difference between subtypes of inward-rectifier K+ channels.

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Species referenced: Xenopus
Genes referenced: kcnj1 kcnj12 kcnj2