A novel force transduction pathway from a tension sensor to the gate in the mechano-gating of MscL channel.
E-coli
MscL
force transduction
gating mechanism
mechanosensitive channel
membrane tension
molecular dynamics
patch clamp
Journal
Frontiers in chemistry
ISSN: 2296-2646
Titre abrégé: Front Chem
Pays: Switzerland
ID NLM: 101627988
Informations de publication
Date de publication:
2023
2023
Historique:
received:
27
02
2023
accepted:
22
05
2023
medline:
22
6
2023
pubmed:
22
6
2023
entrez:
22
6
2023
Statut:
epublish
Résumé
The bacterial mechanosensitive channel of large conductance MscL is activated exclusively by increased tension in the membrane bilayer. Despite many proposed models for MscL opening, its precise mechano-gating mechanism, particularly how the received force at the tension sensor transmits to the gate remains incomplete. Previous studies have shown that along with amphipathic
Identifiants
pubmed: 37347044
doi: 10.3389/fchem.2023.1175443
pii: 1175443
pmc: PMC10279863
doi:
Types de publication
Journal Article
Langues
eng
Pagination
1175443Informations de copyright
Copyright © 2023 Sawada, Nomura, Martinac and Sokabe.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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