Snapin Specifically Up-Regulates Ca_v1.3 Ca²⁺ Channel Variant with a Long Carboxyl Terminus.

ABSTRACT: Ca²⁺ entry through Ca_v1.3 Ca²⁺ channels plays essential roles in diverse physiological events. We employed yeast-two-hybrid (Y2H) assays to mine novel proteins interacting with Ca_v1.3 and found Snapin2, a synaptic protein, as a partner interacting with the long carboxyl terminus (CT_L) of rat Ca_v1.3_L variant. Co-expression of Snapin with Ca_v1.3_L/Ca_vβ₃/α₂δ₂ subunits increased the peak current density or amplitude by about 2-fold in HEK-293 cells and Xenopus oocytes, without affecting voltage-dependent gating properties and calcium-dependent inactivation. However, the Snapin up-regulation effect was not found for rat Ca_v1.3_S

SUBMITTER: Jeong S 

PROVIDER: S-EPMC8537452 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature