β1a490-508, a 19-residue peptide from C-terminal tail of Cav1.1 β1a subunit, potentiates voltage-dependent calcium release in adult skeletal muscle fibers.

ABSTRACT: The α1 and β1a subunits of the skeletal muscle calcium channel, Cav1.1, as well as the Ca(2+) release channel, ryanodine receptor (RyR1), are essential for excitation-contraction coupling. RyR1 channel activity is modulated by the β1a subunit and this effect can be mimicked by a peptide (β1a490-524) corresponding to the 35-residue C-terminal tail of the β1a subunit. Protein-protein interaction assays confirmed a high-affinity interaction between the C-terminal tail of the β1a and RyR1. Based on previous results using overlapping peptides tested on isolated RyR1, we hypothesized that a 19-amino-acid residue peptide (β1a490-508) is sufficient to reproduce activating effects of β1a490-524. Here we examined the effects of β1a490-508 on Ca(2+) release and Ca(2+) currents in adult skeletal muscl

SUBMITTER: Hernandez-Ochoa EO 

PROVIDER: S-EPMC3944469 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature