Cargando…
Physiological CRAC channel activation and pore properties require STIM1 binding to all six Orai1 subunits
The binding of STIM1 to Orai1 controls the opening of store-operated CRAC channels as well as their extremely high Ca(2+) selectivity. Although STIM1 dimers are known to bind directly to the cytosolic C termini of the six Orai1 subunits (SUs) that form the channel hexamer, the dependence of channel...
Autores principales: | Yen, Michelle, Lewis, Richard S. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6168240/ https://www.ncbi.nlm.nih.gov/pubmed/30120197 http://dx.doi.org/10.1085/jgp.201711985 |
Ejemplares similares
-
Orai1 pore residues control CRAC channel inactivation independently of calmodulin
por: Mullins, Franklin M., et al.
Publicado: (2016) -
Correction: Orai1 pore residues control CRAC channel inactivation independently of calmodulin
por: Mullins, Franklin M., et al.
Publicado: (2016) -
Authentic CRAC channel activity requires STIM1 and the conserved portion of the Orai N terminus
por: Derler, Isabella, et al.
Publicado: (2018) -
Photocrosslinking-induced CRAC channel-like Orai1 activation independent of STIM1
por: Maltan, Lena, et al.
Publicado: (2023) -
S417 in the CC3 region of STIM1 is critical for STIM1-Orai1 binding and CRAC channel activation
por: Yu, Tao, et al.
Publicado: (2023)