Assembly mechanisms of the neuronal gap junction channel connexin 36 elucidated by Cryo-EM.
Arch Biochem Biophys
; 754: 109959, 2024 Apr.
Article
de En
| MEDLINE
| ID: mdl-38490311
ABSTRACT
Electrical synapses are essential components of neural circuits. Neuronal signal transduction across electrical synapses is primarily mediated by gap junction channels composed of Connexin36 (Cx36), the lack of which causes impaired electrical coupling between certain neurons including cortical interneurons and thalamic reticular nucleus (TRN) neurons. However, the structural basis underlying Cx36 function and assembly remains elusive. Recently, Lee et al. reported cryo-EM structures of Cx36, thus provided first insights of its gating mechanism. Here, we report a consistent cryo-EM structure of Cx36 determined in parallel, and describe unique interactions underpinning its assembly mechanism in complementary to the competing work. In particular, we found non-canonical electrostatic interactions between protomers from opposing hemichannels and a steric complementary site between adjacent protomers within a hemichannel, which together provide a structural explanation for the assembly specificity in homomeric and heteromeric gap junction channels.
Mots clés
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Synapses électriques
/
Limites:
Humans
Langue:
En
Journal:
Arch Biochem Biophys
Année:
2024
Type de document:
Article
Pays d'affiliation:
Chine