Structure-based site-directed photo-crosslinking analyses of multimeric cell-adhesive interactions of voltage-gated sodium channel ß subunits.
Sci Rep
; 6: 26618, 2016 05 24.
Article
em En
| MEDLINE
| ID: mdl-27216889
ABSTRACT
The ß1, ß2, and ß4 subunits of voltage-gated sodium channels reportedly function as cell adhesion molecules. The present crystallographic analysis of the ß4 extracellular domain revealed an antiparallel arrangement of the ß4 molecules in the crystal lattice. The interface between the two antiparallel ß4 molecules is asymmetric, and results in a multimeric assembly. Structure-based mutagenesis and site-directed photo-crosslinking analyses of the ß4-mediated cell-cell adhesion revealed that the interface between the antiparallel ß4 molecules corresponds to that in the trans homophilic interaction for the multimeric assembly of ß4 in cell-cell adhesion. This trans interaction mode is also employed in the ß1-mediated cell-cell adhesion. Moreover, the ß1 gene mutations associated with generalized epilepsy with febrile seizures plus (GEFS+) impaired the ß1-mediated cell-cell adhesion, which should underlie the GEFS+ pathogenesis. Thus, the structural basis for the ß-subunit-mediated cell-cell adhesion has been established.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Subunidade beta-1 do Canal de Sódio Disparado por Voltagem
/
Subunidade beta-4 do Canal de Sódio Disparado por Voltagem
Limite:
Animals
Idioma:
En
Revista:
Sci Rep
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
Japão