ArticleChannels (Austin, Tex.)
Voltage-dependent conformational changes of KVAP S4 segment in bacterial membrane environment.
Article in Channels (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Structural mechanism of voltage-dependent gating in an isolated voltage-sensing domain.Nature structural & molecular biology · 2014Article
- Structural basis of lipid-driven conformational transitions in the KvAP voltage-sensing domain.Nature structural & molecular biology · 2014Article
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Authors and funding
2 authors.
Funding
Abstract
The nature and magnitude of voltage sensor conformational changes during ion channel activation are controversial. We have analyzed the topology of the K(V)AP voltage sensor domain in the absence and presence of a hyperpolarized voltage using native, right-side out membrane vesicles from E. coli. This approach does not disrupt the normal membrane environment of the channel protein and does not involve detergent solubilization. We found that voltage-dependent conformational changes are focused in the N-terminal half of the K(V)AP S4 segment, in excellent agreement with results obtained with Shaker. Homologous residues in the K(V)AP and Shaker S4 segments are transferred from the extracellular to the intracellular compartment upon hyperpolarization. Taken together with X-ray structures indicating that the K(V)AP S4 segment is outwardly displaced at 0 mV compared to S4 in a mammalian Shaker channel, our results are consistent with the idea that S4 moves further during voltage-dependent activation in K(V)AP than in Shaker.
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