Channel gating dependence on pore lining helix glycine residues in skeletal muscle ryanodine receptor
Y Mei, L Xu, DD Mowrey, RM Giraldez, Y Wang… - Journal of Biological …, 2015 - ASBMB
Type 1 ryanodine receptors (RyR1s) release Ca 2+ from the sarcoplasmic reticulum to
initiate skeletal muscle contraction. The role of RyR1-G4934 and-G4941 in the pore-lining
helix in channel gating and ion permeation was probed by replacing them with amino acid
residues of increasing side chain volume. RyR1-G4934A,-G4941A, and-G4941V mutant
channels exhibited a caffeine-induced Ca 2+ release response in HEK293 cells and bound
the RyR-specific ligand [3 H] ryanodine. In single channel recordings, significant differences …
initiate skeletal muscle contraction. The role of RyR1-G4934 and-G4941 in the pore-lining
helix in channel gating and ion permeation was probed by replacing them with amino acid
residues of increasing side chain volume. RyR1-G4934A,-G4941A, and-G4941V mutant
channels exhibited a caffeine-induced Ca 2+ release response in HEK293 cells and bound
the RyR-specific ligand [3 H] ryanodine. In single channel recordings, significant differences …
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