The quest to map STIM1 activation in granular detail.
Cell Calcium
; 123: 102946, 2024 Nov.
Article
en 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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Molécula de Interacción Estromal 1
/
Proteínas de Neoplasias
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Cell Calcium
Año:
2024
Tipo del documento:
Article
Pais de publicación:
Países Bajos