The amino terminal domain plays an important role in transjunctional voltage-dependent gating kinetics of Cx45 gap junctions.
Action Potentials
Amino Acid Motifs
Amino Acid Sequence
Animals
Cell Line
Connexins
/ chemistry
Gap Junctions
/ metabolism
Genes, Reporter
Humans
Ion Channel Gating
Mice
Models, Molecular
Myocytes, Cardiac
/ metabolism
Protein Binding
Protein Interaction Domains and Motifs
Protein Transport
Structure-Activity Relationship
Gap junction channel
Gating kinetics
Patch clamp
connexin45
Journal
Journal of molecular and cellular cardiology
ISSN: 1095-8584
Titre abrégé: J Mol Cell Cardiol
Pays: England
ID NLM: 0262322
Informations de publication
Date de publication:
06 2020
06 2020
Historique:
received:
07
11
2019
revised:
04
03
2020
accepted:
03
04
2020
pubmed:
24
4
2020
medline:
13
7
2021
entrez:
24
4
2020
Statut:
ppublish
Résumé
Gap junction (GJ) channels formed by Cx45 exist in nodal cells in the heart where the action potential propagation is the slowest. The cellular mechanisms of slow propagation speed (or longer junctional delay) in nodal cells could be a combination of several factors, including lack of voltage-gated sodium channels, smaller cell size, and a lower GJ coupling conductance of Cx45. Compared to other cardiac GJs, Cx45 GJs possess not only the lowest unitary channel conductance, but also the highest extent and the fastest kinetics of the transjunctional voltage-dependent gating (V
Identifiants
pubmed: 32325151
pii: S0022-2828(20)30085-7
doi: 10.1016/j.yjmcc.2020.04.004
pii:
doi:
Substances chimiques
Connexins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
71-84Subventions
Organisme : CIHR
ID : 153415
Pays : Canada
Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest None.