title: Functional reconstitution of purified human Hv1 H+ channels.
abstract: Voltage-dependent H(+) (Hv) channels mediate proton conduction into and out of cells under the control of membrane voltage. Hv channels are unusual compared to voltage-dependent K(+), Na(+), and Ca(2+) channels in that Hv channel genes encode a voltage sensor domain (VSD) without a pore domain. The H(+) currents observed when Hv channels are expressed heterologously suggest that the VSD itself provides the pathway for proton conduction. In order to exclude the possibility that the Hv channel VSD assembles with an as yet unknown protein in the cell membrane as a requirement for H(+) conduction, we have purified Hv channels to homogeneity and reconstituted them into synthetic lipid liposomes. The Hv channel VSD by itself supports H(+) flux.
authors.affiliation: Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.
authors.forename: Seok-Yong
authors.initials: SY
authors.lastname: Lee
authors.forename: James A
authors.initials: JA
authors.lastname: Letts
authors.forename: Roderick
authors.initials: R
authors.lastname: MacKinnon
mesh_terms: D000595:Amino Acid Sequence; D004563:Electrochemistry; D005453:Fluorescence; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007473:Ion Channels / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008081:Liposomes; D011522:Protons; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
chemical_list: C510235:HVCN1 protein, human; D007473:Ion Channels; D008081:Liposomes; D011522:Protons; D011994:Recombinant Proteins