Calcium-dependent block of ryanodine receptor channel of swine skeletal muscle by direct binding of calmodulin
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Cited by (54)
Three-dimensional perspective on ryanodine receptor mutations causing skeletal and cardiac muscle-related diseases
2023, Current Opinion in PharmacologyRyanodine receptors under the magnifying lens: Insights and limitations of cryo-electron microscopy and X-ray crystallography studies
2016, Cell CalciumCitation Excerpt :For RyR1, CaM activates at low Ca2+, but is inhibitory at high Ca2+ concentrations. In RyR2, CaM appears inhibitory at all Ca2+ concentrations [116–119]. The binding of CaM to intact RyRs has not been studied yet at high resolution, but multiple previous reports at low resolution have shown that both apoCaM and Ca2+/CaM can bind to the edge of the cytosolic cap [120,121].
Calmodulin and STIM proteins: Two major calcium sensors in the cytoplasm and endoplasmic reticulum in memory of Professor Koichi Yagi, Hokkaido University.
2015, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Extraordinarily, CaM can function as both a negative and positive feedback regulator for the myriad of Ca2+-signalling toolkit proteins. For example, Ca2+–CaM can bind to and inhibit RyR1 and RyR2 [47–51]. IP3Rs are also inhibited by CaM binding, although data have argued for both Ca2+-dependent [52–54] and –independent [55,56] downregulation [57].
Ryanodine receptors: Allosteric ion channel giants
2015, Journal of Molecular BiologyRyanodine receptors: Structure and function
2012, Journal of Biological ChemistryCitation Excerpt :At high Ca2+ levels, CaM can inhibit both RyR1 and RyR2. At low Ca2+ levels, however, it activates RyR1 but inhibits RyR2 (40–43). Many studies have focused on identifying the sequences in RyRs that can bind CaM.
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On leave from the Laboratorio de Fisiología, Universidad del Bío-Bío, Chillán, Chile.