Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 105, Issue 22, Pages 7692-7695Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0803277105
Keywords
membrane protein; voltage-dependent ion channel; voltage sensor
Categories
Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [GM 43949, R01 GM043949] Funding Source: Medline
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In voltage-gated Na+, K+, and Ca2+ channels, four voltage-sensor domains operate on a central pore domain in response to membrane voltage. In contrast, the voltage-gated proton channel (Hv) contains only a voltage-sensor domain, lacking a separate pore domain. The subunit stoichiometry and organization of Hv has been unknown. Here, we show that human Hv1 forms a dimer in the membrane and define regions that are close to the dimer interface by using cysteine cross-linking. Two dimeric interfaces appear to exist in Hv1, one mediated by S1 and the adjacent extracellular loop, and the other mediated by a putative intracellular coiled-coil domain. It may be significant that Hv1 uses for its dimer interface a surface that corresponds to the interface between the voltage sensor and pore in Kv channels.
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