title: How to open a proton pore-more than S4?
abstract: Pioneering studies in voltage-gated potassium channels have described movement of the voltage-sensing domain (VSD) S4 helix across the membrane electric field in molecular detail, but much less is known regarding opening of the intrinsic proton pore within VSDs of voltage-dependent proton channels. By systematically probing local kinematics, a new study reveals that movements in helix S1 correlate with pore opening and are distinct from voltage-sensing movements of the charged S4 segment.
authors.affiliation: Departments of Neuroscience and Biomolecular Chemistry, University of Wisconsin, Madison, Wisconsin, USA.
authors.forename: Marcel P
authors.initials: MP
authors.lastname: Goldschen-Ohm
authors.affiliation: Departments of Neuroscience and Biomolecular Chemistry, University of Wisconsin, Madison, Wisconsin, USA.
authors.forename: Baron
authors.identifier: 0000000349547034
authors.initials: B
authors.lastname: Chanda
mesh_terms: D000818:Animals; D002938:Ciona intestinalis; D015640:Ion Channel Gating; D007473:Ion Channels / Q000737:chemistry*; D008958:Models, Molecular
chemical_list: D007473:Ion Channels
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