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Article
Nature Neuroscience  6, 353 - 361 (2003)
Published online: 17 March 2003; | doi:10.1038/nn1028

Hyperpolarization moves S4 sensors inward to open MVP, a methanococcal voltage-gated potassium channel

Federico Sesti1, 2, Sindhu Rajan1, Rosana Gonzalez-Colaso1, Natalia Nikolaeva1 & Steve A.N. Goldstein1

1  Departments of Pediatrics and Cellular and Molecular Physiology, Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Avenue, New Haven, Connecticut 06536, USA

2  Present address: UMDNJ-Robert Wood Johnson Medical School, Department of Physiology and Biophysics, 675 Hoes Lane, Piscataway, New Jersey 08854, USA

Correspondence should be addressed to Steve A.N. Goldstein steve.goldstein@yale.edu
MVP, a Methanococcus jannaschii voltage-gated potassium channel, was cloned and shown to operate in eukaryotic and prokaryotic cells. Like pacemaker channels, MVP opens on hyperpolarization using S4 voltage sensors like those in classical channels activated by depolarization. The MVP S4 span resembles classical sensors in sequence, charge, topology and movement, traveling inward on hyperpolarization and outward on depolarization (via canaliculi in the protein that bring the extracellular and internal solutions into proximity across a short barrier). Thus, MVP opens with sensors inward indicating a reversal of S4 position and pore state compared to classical channels. Homolo-gous channels in mammals and plants are expected to function similarly.

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REFERENCE
Calcium Channel Diversity
Nature Encyclopaedia of Life Sciences

REVIEWS
POTASSIUM LEAK CHANNELS AND THE KCNK FAMILY OF TWO-P-DOMAIN SUBUNITS
Nature Reviews Neuroscience Review Article (01 Mar 2001)

RESEARCH
Voltage-sensing mechanism is conserved among ion channels gated by opposite voltages
Nature Letters to Editor (24 Oct 2002)
KCNK2: reversible conversion of a hippocampal potassium leak into a voltage-dependent channel
Nature Neuroscience Article (01 May 2001)

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Nature Neuroscience
ISSN: 1097-6256
EISSN: 1546-1726
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