Subunit organization and functional transitions in Ci-VSP.
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.
Kohout
Susy C
SC
Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
Ulbrich
Maximilian H
MH
Bell
Sarah C
SC
Isacoff
Ehud Y
EY
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
D008565:Membrane Proteins; D011993:Recombinant Fusion Proteins