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Operation of the Voltage Sensor of a Human Voltage- and Ca2+-activated K+ Channel
Department of Anesthesiology, Division of Molecular Medicine, avid Geffen School of Medicine, University of California, Los Angeles, USA.
Department of Anesthesiology, Division of Molecular Medicine, avid Geffen School of Medicine, University of California, Los Angeles, USA.
Department of Anesthesiology, Division of Molecular Medicine, avid Geffen School of Medicine, University of California, Los Angeles, USA.
Department of Anesthesiology, Division of Molecular Medicine, avid Geffen School of Medicine, University of California, Los Angeles, USA.
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2010 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 107, no 9, p. 4459-4464Article in journal (Refereed) Published
Abstract [en]

Voltage sensor domains (VSDs) are structurally and functionally conserved protein modules that consist of four transmembrane segments (S1–S4) and confer voltage sensitivity to many ion channels. Depolarization is sensed by VSD-charged residues residing in the membrane field, inducing VSD activation that facilitates channel gating. S4 is typically thought to be the principal functional component of the VSD because it carries, in most channels, a large portion of the VSD gating charge. The VSDs of large-conductance, voltage- and Ca2+-activated K+ channels are peculiar in that more gating charge is carried by transmembrane segments other than S4. Considering its “decentralized” distribution of voltage-sensing residues, we probed the BKCa VSD for evidence of cooperativity between charge-carrying segments S2 and S4. We achieved this by optically tracking their activation by using voltage clamp fluorometry, in channels with intact voltage sensors and charge-neutralized mutants. The results from these experiments indicate that S2 and S4 possess distinct voltage dependence, but functionally interact, such that the effective valence of one segment is affected by charge neutralization in the other. Statistical-mechanical modeling of the experimental findings using allosteric interactions demonstrates two mechanisms (mechanical coupling and dynamic focusing of the membrane electric field) that are compatible with the observed cross-segment effects of charge neutralization.

Place, publisher, year, edition, pages
National Academy of Sciences , 2010. Vol. 107, no 9, p. 4459-4464
National Category
Biophysics
Identifiers
URN: urn:nbn:se:liu:diva-162173DOI: 10.1073/pnas.0911959107OAI: oai:DiVA.org:liu-162173DiVA, id: diva2:1371947
Available from: 2019-11-21 Created: 2019-11-21 Last updated: 2019-11-22Bibliographically approved

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Pantazis, Antonios
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