Biochemical and Biophysical Research Communications
Regular ArticleCalcium-Dependent Activation of Skeletal-Muscle Ca2+ Release Channel (Ryanodine Receptor) by Calmodulin
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S100A1 protein does not compete with calmodulin for ryanodine receptor binding but structurally alters the ryanodine receptoro·calmodulin complex
2016, Journal of Biological ChemistryCitation Excerpt :Two important modulators of Ca2+ cycling are EF-hand Ca2+-binding proteins, calmodulin (CaM) and S100A1. CaM is well known to directly bind to the RyR isoforms in skeletal (RyR1) and cardiac (RyR2) muscle and modulate channel activity in vitro or in situ (1, 2). S100A1 has also been shown to interact with and functionally modulate RyR1 and RyR2 (3–5).
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 BiologyCitation Excerpt :At high Ca2 + levels, CaM can inhibit both RyR1 and RyR2. At low Ca2 + levels, it activates RyR1 but inhibits RyR2 [129–132]. The importance of this modulation is underscored by the fact that mutations in CaM can also give rise to CPVT, likely the result of altered regulation of RyR2 [95].
Ryanodine receptors: Structure and function
2012, Journal of Biological ChemistryCalmodulin-binding locations on the skeletal and cardiac ryanodine receptors
2012, Journal of Biological ChemistryCitation Excerpt :The stoichiometry of CaM binding is 1 mol of CaM/mol RyR subunit, regardless of whether Ca2+ is bound (6, 7), and a region of the RyR1 amino acid sequence involving residues 3614–3643 (residues 3581–3612 for RyR2) is involved in binding both apo- and Ca2+-CaM (6, 8). Apo-CaM weakly activates RyR1, whereas Ca2+-CaM inhibits RyR1 (9–12). In contrast, for RyR2, CaM inhibits receptor activity at both high and low [Ca2+] (7, 13).