Subunit organization and functional transitions in Ci-VSP

Susy C. Kohout, Maximilian H. Ulbrich, Sarah C. Bell, Ehud Y. Isacoff

Research output: Contribution to journalArticlepeer-review

120 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)106-108
Number of pages3
JournalNature Structural and Molecular Biology
Volume15
Issue number1
DOIs
StatePublished - Jan 2008
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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