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Calmodulin and ATP support activity of the Cav1.2 channel through dynamic interactions with the channel

KEY POINTS: Cav1.2 channels maintain activity through interactions with calmodulin (CaM). In this study, activities of the Cav1.2 channel (α1C) and of mutant‐derivatives, C‐terminal deleted (α1CΔ) and α1CΔ linked with CaM (α1CΔCaM), were compared in the inside‐out mode. α1CΔ with CaM, but not withou...

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Publicado en:J Physiol
Autores principales: Minobe, Etsuko, Mori, Masayuki X., Kameyama, Masaki
Formato: Artigo
Lenguaje:Inglês
Publicado: John Wiley and Sons Inc. 2017
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC5390892/
https://ncbi.nlm.nih.gov/pubmed/28130847
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1113/JP273736
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