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CALM3 — RYR2

Text-mined interactions from Literome

Damiani et al., J Muscle Res Cell Motil 2000 : Pharmacological clues to calmodulin mediated activation of skeletal ryanodine receptor using [ 3H ] -ryanodine binding
Rodney et al., J Biol Chem 2001 : This region of the ryanodine receptor has previously been identified as a site of intersubunit contact, suggesting the possibility that calmodulin regulates ryanodine receptor activity by regulating subunit-subunit interactions
Wu et al., Proc Natl Acad Sci U S A 2001 : Calmodulin kinase (CaMK) has characteristics suitable for an ECC coordinating molecule : it is activated by Ca ( 2+ ) /calmodulin, it regulates LTCC and RyR , and it is enriched in the vicinity of LTCC and RyR
Rodney et al., Biochemistry 2001 : Ca ( 2+ ) -free calmodulin ( apocalmodulin ) activates and Ca ( 2+ ) -calmodulin inhibits the ryanodine receptor
Fruen et al., Biochemistry 2003 : In contrast to the RYR1, no activation of the cardiac RYR2 isoform by wild-type CaM was observed, but rather CaM inhibited the RYR2 at all Ca2+ concentrations ( 100 nM to 1 mM ) ... CaM inhibition of the RYR2 was nonetheless abolished by each of four mutations targeting individual CaM Ca2+ sites ... Furthermore, a mutant CaM deficient in Ca2+ binding at all four Ca2+ sites significantly activated the RYR2 and acted as a competitive inhibitor of RYR2 regulation by wild-type Ca2+CaM
Yamaguchi et al., J Biol Chem 2003 : Here we tested whether CaM regulates RyR2 by binding to a highly conserved site identified previously in RyR1 ... In single channel measurements, deletion of the putative CaM binding site eliminated CaM inhibition of RyR2 at Ca2+ concentrations below and above 1 microm ... The results indicate that CaM regulates RyR1 and RyR2 by binding to a single, highly conserved CaM binding site and that other RyR type-specific sites are likely responsible for the differential functional regulation of RyR1 and RyR2 by CaM
Hill et al., Mol Pharmacol 2004 : Functional regulation of the cardiac ryanodine receptor by suramin and calmodulin involves multiple binding sites
Yamaguchi et al., J Biol Chem 2004 : Calmodulin (CaM) inhibits the skeletal muscle ryanodine receptor-1 ( RyR1 ) and cardiac muscle RyR2 at micromolar Ca ( 2+ ) but activates RyR1 and inhibits RyR2 at submicromolar Ca ( 2+ ) by binding to a single, highly conserved CaM binding site ... To identify regions responsible for the differential regulation of RyR1 and RyR2 by CaM , we generated chimeras encompassing and flanking the CaM binding domain ... They further suggest that five non conserved amino acids in the C-terminal region flanking the CaM binding domain have a key role in CaM inhibition of RyR2
Wolner et al., Br J Pharmacol 2005 (Calcium Signaling...) : As calmodulin activates and inhibits the ryanodine receptor depending on whether Ca2+ is absent or present, suramin analogues were screened for inhibition of the ryanodine receptor
Balog et al., Am J Physiol Heart Circ Physiol 2006 : Site-specific substitution of individual CaM Met residues with Gln demonstrated that Met124 was required for both high-affinity CaM binding to RyR2 and for maximal CaM inhibition
Guo et al., Circ Res 2006 : Ca2+/Calmodulin dependent protein kinase II phosphorylation of ryanodine receptor does affect calcium sparks in mouse ventricular myocytes
Yamaguchi et al., J Clin Invest 2007 (Cardiomegaly) : Studies with isolated membrane fractions have shown that calmodulin (CaM) inhibits the activity of cardiac muscle cell Ca ( 2+ ) release channel ryanodine receptor 2 (RyR2) ... To determine the physiological importance of CaM regulation of RyR2 , we generated a mouse with 3 amino acid substitutions ( RyR2-W3587A/L3591D/F3603A ) in exon 75 of the Ryr2 gene, which encodes the CaM binding site of RyR2 ... Biochemical analysis of hearts of 7- and 10-day-old homozygous mutant mice indicated an impaired CaM inhibition of RyR2 at micromolar Ca ( 2+ ) concentrations, reduction in RyR2 protein levels and sarcoplasmic reticulum Ca ( 2+ ) sequestration, and upregulation of genes and/or proteins associated with class II histone deacetylase/myocyte enhancer factor-2 and calcineurin signaling pathways ... Taken together, the data indicate that impaired CaM inhibition of RyR2 , associated with defective sarcoplasmic reticulum Ca ( 2+ ) release and altered gene expression, leads to cardiac hypertrophy and early death
Sigalas et al., Biophys J 2009 (Ion Channel Gating) : Ca2+-calmodulin increases RyR2 open probability yet reduces ryanoid association with RyR2
Yamaguchi et al., Am J Physiol Heart Circ Physiol 2011 (Cardiomegaly) : The results indicate that an impaired calmodulin regulation of RyR2 was neither associated with an altered CNA-ß/NFAT, class II histone deacetylase (HDAC)/MEF2, nor Akt signaling in embryonic day 16.5 hearts ; rather increased Erk1/2 and p90RSK phosphorylation levels likely leading to reduced GSK-3ß activity were found to precede development of cardiac hypertrophy in mice expressing dysfunctional ryanodine receptor ion channel
Chu et al., Biochemistry 1990 : Calmodulin dependent phosphorylation of the ryanodine receptor protein was unambiguously demonstrated by Western blot analysis
Prosser et al., Cell Calcium 2011 : S100A1 and calmodulin regulation of ryanodine receptor in striated muscle
Guo et al., Biophys J 2011 : However, the structural basis of CaM regulation of the RyR2 is poorly defined, and the presence of other potential CaM binding partners in cardiac myocytes complicates resolution of CaM 's regulatory interactions with RyR2
Hino et al., Cardiovasc Res 2012 (Calcium Signaling...) : Expression of the CaM isoform Gly-Ser-His-CaM ( GSH-CaM ), which has much higher binding affinity than wild-type CaM for RyR1, restored normal CaM binding to RyR2 in both SR and myocytes of failing hearts
Lee et al., Nature 1994 : Cyclic ADP ribose activation of the ryanodine receptor is mediated by calmodulin
Strand et al., Biochim Biophys Acta 1993 : Phosphorylation of the cardiac muscle ryanodine receptor in the presence of either cAMP-PK or calmodulin ( 6.4 and 10.6 pmol Pi/mg SR respectively ) was approximately equal to or twice the [ 3H ] ryanodine binding activity of this preparation ( 5.2 pmol/mg )
Dulhunty et al., Acta Physiol Scand 1996 : Effects of phosphorylation, calmodulin , triadin, calsequestrin and interactions with the alpha 1 subunit of the dihydropyridine receptor on ryanodine receptor activity are summarized
O'Driscoll et al., Biochem J 1996 (Malignant Hyperthermia) : To determine if an abnormal calmodulin (CaM) regulation of the SR Ca ( 2+ ) -release-channel-ryanodine-receptor complex ( RYR1 ) contributes to this hypersensitivity, we investigated the effect of CaM on high-affinity [ 3H ] ryanodine binding to isolated SR vesicles from normal and MHS pig skeletal muscle