The N-terminal domain of the IP3 receptor gates store-operated hTrp3 channels.
Mol Cell
; 4(3): 423-9, 1999 Sep.
Article
en En
| MEDLINE
| ID: mdl-10518223
ABSTRACT
In the present work, we studied the interaction and effect of several IP3 receptor (IP3R) constructs on the gating of the store-operated (SOC) hTrp3 channel. Full-length IP3R coupled to silent hTrp3 channels in intact cells but did not activate them until stores were depleted of Ca2+. By contrast, constructs containing the IP3-binding domain activated silent hTrp3 channels in unstimulated cells and restored gating of hTrp3 by IP3 in excised plasma membrane patches. We conclude that the N-terminal domain of the IP3R functions as a gate and is sufficient for activation of SOCs. The sensing and transduction domains of the IP3R are required to maintain SOCs in an inactive state.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Canales de Calcio
/
Activación del Canal Iónico
/
Calcio
/
Receptores Citoplasmáticos y Nucleares
Límite:
Humans
Idioma:
En
Revista:
Mol Cell
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
1999
Tipo del documento:
Article
País de afiliación:
Estados Unidos