Structural Determinants of Skeletal Muscle Ryanodine Receptor Gating*

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Structural determinants of skeletal muscle ryanodine receptor gating.

Ryanodine receptor type 1 (RyR1) releases Ca(2+) from intracellular stores upon nerve impulse to trigger skeletal muscle contraction. Effector binding at the cytoplasmic domain tightly controls gating of the pore domain of RyR1 to release Ca(2+). However, the molecular mechanism that links effector binding to channel gating is unknown due to lack of structural data. Here, we used a combination ...

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Ryanodine receptor purified from crayfish skeletal muscle.

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Channel Gating Dependence on Pore Lining Helix Glycine Residues in Skeletal Muscle Ryanodine Receptor.

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+) relea...

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Ryanodine Receptor Permeation and Gating

Schneider (1999) recently addressed the question of whether Ca 2 1 sparks arise from the opening of a single ryanodine receptor (RyR) channel or the simultaneous opening of several channels. The discussion highlighted the importance of single RyR channel permeation and gating in the interpretation of Ca 2 1 spark data. The Schneider (1999) perspective inspired us to extend this theoretical disc...

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A Structural Model of the Pore-Forming Region of the Skeletal Muscle Ryanodine Receptor (RyR1)

Ryanodine receptors (RyRs) are ion channels that regulate muscle contraction by releasing calcium ions from intracellular stores into the cytoplasm. Mutations in skeletal muscle RyR (RyR1) give rise to congenital diseases such as central core disease. The absence of high-resolution structures of RyR1 has limited our understanding of channel function and disease mechanisms at the molecular level...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2013

ISSN: 0021-9258

DOI: 10.1074/jbc.m112.433789