A structural determinant of differential sensitivity of cloned inward rectifier 
K+ channels to intracellular spermine

Fakler, Bernd; Brändle, Uwe; Bond, Chris T.; Glowatzki, Elisabeth; König, C.; Adelman, John P.; Zenner, Hans−Peter; Ruppersberg, J. Peter

doi:10.1016/0014-5793(94)01258-X

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A structural determinant of differential sensitivity of cloned inward rectifier K+ channels to intracellular spermine

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Ruppersberg, J. Peter
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Fakler, B., Brändle, U., Bond, C. T., Glowatzki, E., König, C., Adelman, J. P., et al. (1994). A structural determinant of differential sensitivity of cloned inward rectifier K+ channels to intracellular spermine. FEBS Letters, 356(2), 199-203. doi:10.1016/0014-5793(94)01258-X.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-A890-6

Abstract

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.