Negatively charged residues in the first extracellular loop of the L-type Ca_V1.2 channel anchor the interaction with the Ca_Vα2δ1 auxiliary subunit.

ABSTRACT: Voltage-gated L-type Ca_V1.2 channels in cardiomyocytes exist as heteromeric complexes. Co-expression of Ca_Vα2δ1 with Ca_Vβ/Ca_Vα1 proteins reconstitutes the functional properties of native L-type currents, but the interacting domains at the Ca_V1.2/Ca_Vα2δ1 interface are unknown. Here, a homology-based model of Ca_V1.2 identified protein interfaces between the extracellular domain of Ca_Vα2δ1 and the extracellular loops of the Ca_Vα1 protein in repeats I (IS1S2 and IS5S6), II (IIS5S6), and III (IIIS5S6). Insertion of a 9-residue hemagglutinin epitope in IS1S2, but not in IS5S6 or in IIS5S6, prevented the co-immunoprecipitation of Ca_V1.2 with Ca_Vα2δ1. IS1S2 contains a cluster of

SUBMITTER: Bourdin B 

PROVIDER: S-EPMC5655503 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature