Key result
Mutations in the TM10 sequence of the RyR2 channel abolished or reduced sensitivity to activation by caffeine and altered sensitivity to Ca2+, indicating its essential role in channel activation.
Population
Human embryonic kidney 293 cells expressing mouse cardiac ryanodine receptor (RyR2) wild type and TM10 mutants
Comparison
Mutations of each residue within the 24-amino… vs RyR2 wild type
Design
Preclinical
Authors
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TM10 mutations alter RyR2 gating; hypothesis-generating for channelopathies, clinical translation premature.
The TM10 sequence of the cardiac ryanodine receptor is crucial for channel activation and gating, functioning as the pore inner helix.
Wang et al. (2004) studied this question. TM10 sequence mutations vs. RyR2 wild type was evaluated on Channel activation by caffeine and Ca2+. Mutations in the TM10 sequence of the RyR2 channel abolished or reduced sensitivity to activation by caffeine and altered sensitivity to Ca2+, indicating its essential role in channel activation.
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