The quest to map STIM1 activation in granular detail.
Cell Calcium
; 123: 102946, 2024 Nov.
Article
em En
| MEDLINE
| ID: mdl-39226840
ABSTRACT
The conformational change in STIM1 that communicates sensing of ER calcium-store depletion from the STIM ER-luminal domain to the STIM cytoplasmic region and ultimately to ORAI channels in the plasma membrane is broadly understood. However, the structural basis for the STIM luminal-domain dimerization that drives the conformational change has proven elusive. A recently published study has approached this question via molecular dynamics simulations. The report pinpoints STIM residues that may be part of a luminal-domain dimerization interface, and provides unexpected insight into how torsional movements of the STIM luminal domains might trigger release of the cytoplasmic SOAR/CAD domain from its resting tethers to the STIM CC1 segments.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Molécula 1 de Interação Estromal
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Cell Calcium
Ano de publicação:
2024
Tipo de documento:
Article
País de publicação:
Holanda