May 22, 2015Journal of Biological ChemistryOpen Access

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

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Population

HEK293 cells expressing wild-type and mutant Type 1 ryanodine receptors (RyR1)

Comparison

Mutagenesis of RyR1-G4934 and -G4941 vs Wild-type RyR1 (RyR1-WT)

Design

Preclinical

Authors

YMYingwu MeiZhengzhou University LXLe XuChina West Normal University DMDavid D. MowreyAdamas Pharmaceuticals (United States)

Discussion

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Implication

RyR1 pore mutants retain Ca2+ release function; extends mechanistic insights into gating but leaves open disease relevance.

Structured PICO

Population

HEK293 cells expressing wild-type and mutant Type 1 ryanodine receptors (RyR1)

Intervention

Mutagenesis of RyR1-G4934 and -G4941 (G4934A, G4941A, G4941V, G4934V, G4941I)

Comparator

Wild-type RyR1 (RyR1-WT)

Outcome

Channel gating, ion permeation, caffeine-induced Ca2+ release, [3H]ryanodine binding, and protein stabilitysurrogate

Glycine residues in the pore-lining helix of skeletal muscle RyR1 are essential for channel function by providing flexibility and minimizing amino acid clashes.

Cite This Study

Mei et al. (2015) studied this question.

synapsesocial.com/papers/6a993296ea8974fe8c273f9f https://doi.org/10.1074/jbc.m115.659672

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

Discussion

Member takes

Implication

Structured PICO

Cite This Study

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

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider