Proteolytic cleavage of the hydrophobic domain in the Ca_Vα2δ1 subunit improves assembly and activity of cardiac Ca_V1.2 channels.

ABSTRACT: Voltage-gated L-type Ca_V1.2 channels in cardiomyocytes exist as heteromeric complexes with the pore-forming Ca_Vα1, Ca_Vβ, and Ca_Vα2δ1 subunits. The full complement of subunits is required to reconstitute the native-like properties of L-type Ca²⁺ currents, but the molecular determinants responsible for the formation of the heteromeric complex are still being studied. Enzymatic treatment with phosphatidylinositol-specific phospholipase C, a phospholipase C specific for the cleavage of glycosylphosphatidylinositol (GPI)-anchored proteins, disrupted plasma membrane localization of the cardiac Ca_Vα2δ1 prompting us to investigate deletions of its hydrophobic transmembrane domain. Patch-clamp experiments indicated that the C-termina

SUBMITTER: Segura E 

PROVIDER: S-EPMC5491792 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature