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

Publication ,  Journal Article
Lee, S-Y; Letts, JA; Mackinnon, R
Published in: Proc Natl Acad Sci U S A
June 3, 2008

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.

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Published In

Proc Natl Acad Sci U S A

DOI

EISSN

1091-6490

Publication Date

June 3, 2008

Volume

105

Issue

22

Start / End Page

7692 / 7695

Location

United States

Related Subject Headings

  • Protein Subunits
  • Protein Structure, Tertiary
  • Mutation
  • Molecular Sequence Data
  • Ion Channels
  • Humans
  • Dimerization
  • Cysteine
  • Cell Membrane
  • Cell Line
 

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Lee, S.-Y., Letts, J. A., & Mackinnon, R. (2008). Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1. Proc Natl Acad Sci U S A, 105(22), 7692–7695. https://doi.org/10.1073/pnas.0803277105
Lee, Seok-Yong, James A. Letts, and Roderick Mackinnon. “Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1.Proc Natl Acad Sci U S A 105, no. 22 (June 3, 2008): 7692–95. https://doi.org/10.1073/pnas.0803277105.
Lee S-Y, Letts JA, Mackinnon R. Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1. Proc Natl Acad Sci U S A. 2008 Jun 3;105(22):7692–5.
Lee, Seok-Yong, et al. “Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1.Proc Natl Acad Sci U S A, vol. 105, no. 22, June 2008, pp. 7692–95. Pubmed, doi:10.1073/pnas.0803277105.
Lee S-Y, Letts JA, Mackinnon R. Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1. Proc Natl Acad Sci U S A. 2008 Jun 3;105(22):7692–7695.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

EISSN

1091-6490

Publication Date

June 3, 2008

Volume

105

Issue

22

Start / End Page

7692 / 7695

Location

United States

Related Subject Headings

  • Protein Subunits
  • Protein Structure, Tertiary
  • Mutation
  • Molecular Sequence Data
  • Ion Channels
  • Humans
  • Dimerization
  • Cysteine
  • Cell Membrane
  • Cell Line