Interaction via a key tryptophan in the I-II linker of N-type calcium channels is required for beta1 but not for palmitoylated beta2, implicating an additional binding site in the regulation of channel voltage-dependent properties.

ABSTRACT: The CaVbeta subunits of voltage-gated calcium channels regulate these channels in several ways. Here we investigate the role of these auxiliary subunits in the expression of functional N-type channels at the plasma membrane and in the modulation by G-protein-coupled receptors of this neuronal channel. To do so, we mutated tryptophan 391 to an alanine within the alpha-interacting domain (AID) in the I-II linker of CaV2.2. We showed that the mutation W391 virtually abolishes the binding of CaVbeta1b and CaVbeta2a to the CaV2.2 I-II linker and strongly reduced current density and cell surface expression of both CaV2.2/alpha2delta-2/beta1b and/beta2a channels. When associated with CaVbeta1b, the W391A mutation also prevented the CaVbeta1b-mediated hyperpolarization of CaV2.2 channel activation

SUBMITTER: Leroy J 

PROVIDER: S-EPMC6724838 | biostudies-literature | 2005 Jul

REPOSITORIES: biostudies-literature