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Publication : Identification and molecular localization of a pH-sensing domain for the inward rectifier potassium channel HIR.

First Author  Coulter KL Year  1995
Journal  Neuron Volume  15
Issue  5 Pages  1157-68
PubMed ID  7576658 Mgi Jnum  J:29879
Mgi Id  MGI:77403 Doi  10.1016/0896-6273(95)90103-5
Citation  Coulter KL, et al. (1995) Identification and molecular localization of a pH-sensing domain for the inward rectifier potassium channel HIR. Neuron 15(5):1157-68
abstractText  Inward rectifier potassium channels are found in the heart and CNS, where they are critical for the modulation and maintenance of cellular excitability. We present evidence that the inward rectifier potassium channel HIR is modulated by extracellular pH in the physiological range. We show that proton-induced changes in HIR single-channel conductance underlie the HIR pH sensitivity seen on the macroscopic level. We used chimeric and mutant channels to localize the molecular determinant of HIR pH sensitivity to a single residue, H117, in the M1-to-H5 linker region. This residue provides a molecular context that allows a titratable group to influence pore properties. We present evidence that this titratable group is one of two cysteines located in the M1-to-H5 and H5-to-M2 linkers.
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