The cytoplasmic coiled-coil mediates cooperative gating temperature sensitivity in the voltage-gated H(+) channel Hv1.

Nature Communications
Yuichiro FujiwaraYasushi Okamura

Abstract

Hv1/VSOP is a dimeric voltage-gated H(+) channel in which the gating of one subunit is reportedly coupled to that of the other subunit within the dimer. The molecular basis for dimer formation and intersubunit coupling, however, remains unknown. Here we show that the carboxy terminus ends downstream of the S4 voltage-sensor helix twist in a dimer coiled-coil architecture, which mediates cooperative gating. We also show that the temperature-dependent activation of H(+) current through Hv1/VSOP is regulated by thermostability of the coiled-coil domain, and that this regulation is altered by mutation of the linker between S4 and the coiled-coil. Cooperative gating within the dimer is also dependent on the linker structure, which circular dichroism spectrum analysis suggests is α-helical. Our results indicate that the cytoplasmic coiled-coil strands form continuous α-helices with S4 and mediate cooperative gating to adjust the range of temperatures over which Hv1/VSOP operates.

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Citations

Dec 20, 2013·Journal of the Royal Society, Interface·Thomas E DeCoursey, Jonathan Hosler
Feb 26, 2014·The Journal of General Physiology·Yuichiro FujiwaraYasushi Okamura
Mar 4, 2014·Nature Structural & Molecular Biology·Kohei TakeshitaAtsushi Nakagawa
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Nov 21, 2012·The Journal of Physiology·Yuichiro FujiwaraYasushi Okamura
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Aug 24, 2018·Proceedings of the National Academy of Sciences of the United States of America·Thomas E DeCoursey
May 15, 2013·The Journal of Biological Chemistry·Yuichiro FujiwaraYasushi Okamura

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