Subunit organization and functional transitions in Ci-VSP
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Updated: Jul 9, 2026

Utilization of Grafix for the Detection of Transient Interactors of Saccharomyces cerevisiae Spliceosome Subcomplexes
Published on: November 9, 2020
Susy C Kohout1, Maximilian H Ulbrich, Sarah C Bell
1Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
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.
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