Dimerization mechanism of an inverted-topology ion channel in membranes.
Fluc
computational modeling
dimerization
ion channel
single-molecule microscopy
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:
21 Nov 2023
21 Nov 2023
Historique:
pmc-release:
13
05
2024
medline:
15
11
2023
pubmed:
13
11
2023
entrez:
13
11
2023
Statut:
ppublish
Résumé
Many ion channels are multisubunit complexes where oligomerization is an obligatory requirement for function as the binding axis forms the charged permeation pathway. However, the mechanisms of in-membrane assembly of thermodynamically stable channels are largely unknown. Here, we demonstrate a key advance by reporting the dimerization equilibrium reaction of an inverted-topology, homodimeric fluoride channel Fluc in lipid bilayers. While the wild-type channel is a long-lived dimer, we leverage a known mutation, N43S, that weakens Na
Identifiants
pubmed: 37956279
doi: 10.1073/pnas.2308454120
pmc: PMC10666096
doi:
Substances chimiques
Lipid Bilayers
0
Fluorides
Q80VPU408O
Ion Channels
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2308454120Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM128768
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM120260
Pays : United States
Commentaires et corrections
Type : UpdateOf
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