Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1.

Published

Journal Article

In voltage-gated Na(+), K(+), and Ca(2+) 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.

Full Text

Duke Authors

Cited Authors

  • Lee, S-Y; Letts, JA; Mackinnon, R

Published Date

  • June 3, 2008

Published In

Volume / Issue

  • 105 / 22

Start / End Page

  • 7692 - 7695

PubMed ID

  • 18509058

Pubmed Central ID

  • 18509058

Electronic International Standard Serial Number (EISSN)

  • 1091-6490

Digital Object Identifier (DOI)

  • 10.1073/pnas.0803277105

Language

  • eng

Conference Location

  • United States