title: Subunit organization and functional transitions in Ci-VSP.
abstract: Voltage-sensing domains (VSDs) confer voltage dependence on effector domains of membrane proteins. Ion channels use four VSDs to control a gate in the pore domain, but in the recently discovered phosphatase Ci-VSP, the number of subunits has been unknown. Using single-molecule microscopy to count subunits and voltage clamp fluorometry to detect structural dynamics, we found Ci-VSP to be a monomer, which operates independently, but nevertheless undergoes multiple voltage-dependent conformational transitions.
authors: Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
authors: Susy C
authors: SC
authors: Kohout
authors: Maximilian H
authors: MH
authors: Ulbrich
authors: Sarah C
authors: SC
authors: Bell
authors: Ehud Y
authors: EY
authors: Isacoff
mesh_terms: D000818:Animals; D004563:Electrochemistry / Q000379:methods; D005260:Female; D017930:Genes, Reporter; D008565:Membrane Proteins / Q000737:chemistry* / Q000502:physiology*; D008958:Models, Molecular; D009865:Oocytes / Q000502:physiology; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry
chemical_list: D008565:Membrane Proteins; D011993:Recombinant Fusion Proteins