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Cav3.2 calcium channel interactions with the epithelial sodium channel ENaC.


ABSTRACT: This study describes the functional interaction between Cav3.2 calcium channels and the Epithelial Sodium Channel (ENaC). ?-ENaC subunits showed overlapping expression with endogenous Cav3.2 calcium channels in the thalamus and hypothalamus as detected by immunostaining. Moreover, ?- and ?-ENaC subunits could be co-immunoprecipitated with Cav3.2 calcium channels from brain lysates, dorsal horn and lumbar dorsal root ganglia. Mutation of a cluster of lysines present in the intracellular N-terminus region of ?-ENaC (K4R/ K5R/ K9R/ K16R/ K23R) reduced interactions with Cav3.2 calcium channels. ???-ENaC channels enhanced Cav3.2 calcium channel trafficking to the plasma membrane in tsA-201 cells. This effect was reciprocal such that Cav3.2 channel expression also enhanced ?-ENaC trafficking to the cell surface. T-type current density was increased when fully assembled ???-ENaC channels were transiently expressed in CAD cells, a neuronal derived cell line. Altogether, these findings reveal ENaC as an interactor and potential regulator of Cav3.2 calcium channels expressed in neuronal tissues.

SUBMITTER: Garcia-Caballero A 

PROVIDER: S-EPMC6368719 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature

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Cav3.2 calcium channel interactions with the epithelial sodium channel ENaC.

Garcia-Caballero Agustin A   Gandini Maria A MA   Huang Shuo S   Chen Lina L   Souza Ivana A IA   Dang Yan L YL   Stutts M Jackson MJ   Zamponi Gerald W GW  

Molecular brain 20190208 1


This study describes the functional interaction between Cav3.2 calcium channels and the Epithelial Sodium Channel (ENaC). β-ENaC subunits showed overlapping expression with endogenous Cav3.2 calcium channels in the thalamus and hypothalamus as detected by immunostaining. Moreover, β- and γ-ENaC subunits could be co-immunoprecipitated with Cav3.2 calcium channels from brain lysates, dorsal horn and lumbar dorsal root ganglia. Mutation of a cluster of lysines present in the intracellular N-terminu  ...[more]

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