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BertrandD.Devillers-ThiéryA.RevahF.GalziJ.L.HussyN.MulleC.BertrandS.BallivetM.ChangeuxJ.P. 1992 Unconventional pharmacology of a neuronal nicotinic receptor mutated in the channel domain. Proc. Natl. Acad. Sci. USA. 89:1261–1265 10.1073/pnas.89.4.12611741378BertrandD.Devillers-ThiéryA.RevahF.GalziJ.L.HussyN.MulleC.BertrandS.BallivetM.ChangeuxJ.P. 1992 Unconventional pharmacology of a neuronal nicotinic receptor mutated in the channel domain. Proc. Natl. Acad. Sci. USA. 89:1261–1265 10.1073/pnas.89.4.12611741378, BertrandD.Devillers-ThiéryA.RevahF.GalziJ.L.HussyN.MulleC.BertrandS.BallivetM.ChangeuxJ.P. 1992 Unconventional pharmacology of a neuronal nicotinic receptor mutated in the channel domain. Proc. Natl. Acad. Sci. USA. 89:1261–1265 10.1073/pnas.89.4.12611741378
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Lei Hu, Jingyi Shi, Zhongming Ma, G. Krishnamoorthy, F. Sieling, Guangping Zhang, F. Horrigan, J. Cui (2003)
Participation of the S4 voltage sensor in the Mg2+-dependent activation of large conductance (BK) K+ channelsProceedings of the National Academy of Sciences of the United States of America, 100
MthK is a Ca 2+ -gated K + channel whose activity is inhibited by cytoplasmic H + . To determine possible mechanisms underlying the channel’s proton sensitivity and the relation between H + inhibition and Ca 2+ -dependent gating, we recorded current through MthK channels incorporated into planar lipid bilayers. Each bilayer recording was obtained at up to six different Ca 2+ (ranging from nominally 0 to 30 mM) at a given H + , in which the solutions bathing the cytoplasmic side of the channels were changed via a perfusion system to ensure complete solution exchanges. We observed a steep relation between Ca 2+ and open probability (Po), with a mean Hill coefficient (n H ) of 9.9 ± 0.9. Neither the maximal Po (0.93 ± 0.005) nor n H changed significantly as a function of H + over pH ranging from 6.5 to 9.0. In addition, MthK channel activation in the nominal absence of Ca 2+ was not H + sensitive over pH ranging from 7.3 to 9.0. However, increasing H + raised the EC 50 for Ca 2+ activation by ∼4.7-fold per tenfold increase in H + , displaying a linear relation between log(EC 50 ) and log(H + ) (i.e., pH) over pH ranging from 6.5 to 9.0. Collectively, these results suggest that H + binding does not directly modulate either the channel’s closed–open equilibrium or the allosteric coupling between Ca 2+ binding and channel opening. We can account for the Ca 2+ activation and proton sensitivity of MthK gating quantitatively by assuming that Ca 2+ allosterically activates MthK, whereas H + opposes activation by destabilizing the binding of Ca 2+ . Footnotes Abbreviations used in this paper: BK large-conductance Ca 2+ -activated K + CHES 2- N -cyclohexylaminoethanesulfonic acid DM decyl maltoside Po open probability MWC Monod-Wyman-Changeux Submitted: 18 December 2009 Accepted: 13 April 2010 This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms ). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/ ).
The Journal of General Physiology – Rockefeller University Press
Published: May 1, 2010
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