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The RCK1 Domain of the Human BKCa Channel Transduces Ca2+ Binding into Structural Rearrangements
Division of Molecular Medicine, Department of Anesthesiology, David Geffen School of Medicine at University of California, Los Angeles, USA.
Division of Molecular Medicine, Department of Anesthesiology, David Geffen School of Medicine at University of California, Los Angeles, USA.
Division of Molecular Medicine, Department of Anesthesiology, David Geffen School of Medicine at University of California, Los Angeles, USA.
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, USA.
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2010 (English)In: The Journal of General Physiology, ISSN 0022-1295, E-ISSN 1540-7748, Vol. 136, no 2, p. 189-202Article in journal (Refereed) Published
Abstract [en]

Large-conductance voltage- and Ca2+-activated K+ (BKCa) channels play a fundamental role in cellular function by integrating information from their voltage and Ca2+ sensors to control membrane potential and Ca2+ homeostasis. The molecular mechanism of Ca2+-dependent regulation of BKCa channels is unknown, but likely relies on the operation of two cytosolic domains, regulator of K+ conductance (RCK)1 and RCK2. Using solution-based investigations, we demonstrate that the purified BKCa RCK1 domain adopts an α/β fold, binds Ca2+, and assembles into an octameric superstructure similar to prokaryotic RCK domains. Results from steady-state and time-resolved spectroscopy reveal Ca2+-induced conformational changes in physiologically relevant [Ca2+]. The neutralization of residues known to be involved in high-affinity Ca2+ sensing (D362 and D367) prevented Ca2+-induced structural transitions in RCK1 but did not abolish Ca2+ binding. We provide evidence that the RCK1 domain is a high-affinity Ca2+ sensor that transduces Ca2+ binding into structural rearrangements, likely representing elementary steps in the Ca2+-dependent activation of human BKCa channels.

Place, publisher, year, edition, pages
Rockefeller University Press, 2010. Vol. 136, no 2, p. 189-202
National Category
Structural Biology
Identifiers
URN: urn:nbn:se:liu:diva-162174DOI: 10.1085/jgp.200910374OAI: oai:DiVA.org:liu-162174DiVA, id: diva2:1371951
Available from: 2019-11-21 Created: 2019-11-21 Last updated: 2019-11-26Bibliographically approved

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Pantazis, Antonios

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