Molecular moieties masking Ca²⁺-dependent facilitation of voltage-gated Ca_v2.2 Ca²⁺ channels.

ABSTRACT: Voltage-gated Ca_v2.1 (P/Q-type) Ca²⁺ channels undergo Ca²⁺-dependent inactivation (CDI) and facilitation (CDF), both of which contribute to short-term synaptic plasticity. Both CDI and CDF are mediated by calmodulin (CaM) binding to sites in the C-terminal domain of the Ca_v2.1 α₁ subunit, most notably to a consensus CaM-binding IQ-like (IQ) domain. Closely related Ca_v2.2 (N-type) channels display CDI but not CDF, despite overall conservation of the IQ and additional sites (pre-IQ, EF-hand-like [EF] domain, and CaM-binding domain) that regulate CDF of Ca_v2.1. Here we investigate the molecular determinants that prevent Ca_v2.2 channels from undergoing CDF. Although alternative splicing of C-terminal exons

SUBMITTER: Thomas JR 

PROVIDER: S-EPMC5749111 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature