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The response of the tandem pore potassium channel TASK-3 (K2P9.1) to voltage : gating at the cytoplasmic mouth

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Ashmole, I., Vavoulis, Dimitris V., Stansfeld, P. J., Mehta, Puja R., Feng, Jianfeng, Sutcliffe, M. J. and Stanfield, Peter R.. (2009) The response of the tandem pore potassium channel TASK-3 (K2P9.1) to voltage : gating at the cytoplasmic mouth. Journal of Physiology, The, Vol.587 . pp. 4769-4783. ISSN 0022-3751

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Official URL: http://dx.doi.org/10.1113/jphysiol.2009.175430

Abstract

Although the tandem pore potassium channel TASK-3 is thought to open and shut at its selectivity filter in response to changes of extracellular pH, it is currently unknown whether the channel also shows gating at its inner, cytoplasmic mouth through movements of membrane helices M2 and M4.We used two electrode voltage clamp and single channel recording to show that TASK-3 responds to voltage in a way that reveals such gating. In wild-type channels, Popen was very low at negative voltages, but increased with depolarisation. The effect of voltage was relatively weak and the gating charge small, ∼0.17.Mutants A237T (in M4) and N133A (in M2) increased Popen at a given voltage, increasing mean open time and the number of openings per burst. In addition, the relationship between Popen andvoltagewas shifted to lesspositive voltages. Mutation of putative hinge glycines (G117A, G231A), residues that are conserved throughout the tandem pore channel family, reduced Popen at a given voltage, shifting the relationship with voltage to a more positive potential range. None of these mutants substantially affected the response of the channel to extracellular acidification. We have used the results from single channel recording to develop a simple kinetic model to show how gating occurs through two classes of conformation change, with two routes out of the open state, as expected if gating occurs both at the selectivity filter and at its cytoplasmic mouth.

Item Type:	Journal Article
Subjects:	Q Science > QP Physiology
Divisions:	Faculty of Science > Centre for Scientific Computing Faculty of Science > Computer Science Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)
Library of Congress Subject Headings (LCSH):	Potassium channels, Cytoplasm, Acids -- Physiological effect
Journal or Publication Title:	Journal of Physiology, The
Publisher:	Wiley-Blackwell Publishing Ltd.
ISSN:	0022-3751
Date:	15 October 2009
Volume:	Vol.587
Page Range:	pp. 4769-4783
Identification Number:	10.1113/jphysiol.2009.175430
Status:	Peer Reviewed
Access rights to Published version:	Open Access
Funder:	Wellcome Trust (London, England)
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URI:	http://wrap.warwick.ac.uk/id/eprint/3046