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 language | English (US) |
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Pages (from-to) | 106-108 |
Number of pages | 3 |
Journal | Nature Structural and Molecular Biology |
Volume | 15 |
Issue number | 1 |
DOIs | |
State | Published - Jan 2008 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology