Voltage-sensor movements in the Eag Kv channel under an applied electric field.
Eag channel
cryo-EM
membrane potential
potassium channel
voltage sensor
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
16 Nov 2022
16 Nov 2022
Historique:
entrez:
4
11
2022
pubmed:
5
11
2022
medline:
9
11
2022
Statut:
ppublish
Résumé
Voltage-dependent ion channels regulate the opening of their pores by sensing the membrane voltage. This process underlies the propagation of action potentials and other forms of electrical activity in cells. The voltage dependence of these channels is governed by the transmembrane displacement of the positive charged S4 helix within their voltage-sensor domains. We use cryo-electron microscopy to visualize this movement in the mammalian Eag voltage-dependent potassium channel in lipid membrane vesicles with a voltage difference across the membrane. Multiple structural configurations show that the applied electric field displaces S4 toward the cytoplasm by two helical turns, resulting in an extended interfacial helix near the inner membrane leaflet. The position of S4 in this down conformation is sterically incompatible with an open pore, thus explaining how movement of the voltage sensor at hyperpolarizing membrane voltages locks the pore shut in this kind of voltage-dependent K
Identifiants
pubmed: 36331999
doi: 10.1073/pnas.2214151119
pmc: PMC9674223
doi:
Substances chimiques
Potassium Channels, Voltage-Gated
0
Lipid Bilayers
0
Potassium Channels
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2214151119Subventions
Organisme : Howard Hughes Medical Institute (HHMI)
ID : HHMI
Commentaires et corrections
Type : CommentIn
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