Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor).

@article{Balshaw2001CalmodulinBA,
  title={Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor).},
  author={David M. Balshaw and Le Xu and Naohiro Yamaguchi and Daniel A. Pasek and Gerhard Meissner},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 23},
  pages={20144-53}
}
Metabolically (35)S-labeled calmodulin (CaM) was used to determine the CaM binding properties of the cardiac ryanodine receptor (RyR2) and to identify potential channel domains for CaM binding. In addition, regulation of RyR2 by CaM was assessed in [(3)H]ryanodine binding and single-channel measurements. Cardiac sarcoplasmic reticulum vesicles bound approximately four CaM molecules per RyR2 tetramer in the absence of Ca(2+); in the presence of 100 microm Ca(2+), the vesicles bound 7.5 CaM… CONTINUE READING

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