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CALM3 — RYR1

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., Biochemistry 2000 : Regulation of RYR1 activity by Ca ( 2+ ) and calmodulin ... We demonstrate that Ca ( 2+ ) -free calmodulin enhances the affinity of RYR1 for Ca ( 2+ ) while Ca ( 2+ ) binding to calmodulin converts calmodulin from an activator to an inhibitor
Rodney et al., J Biol Chem 2001 : The skeletal muscle calcium release channel , ryanodine receptor, is activated by calcium-free calmodulin and inhibited by calcium bound calmodulin ... 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
Zhao et al., J Biol Chem 2001 : Dantrolene inhibition of the RYR1 was dependent on the presence of the adenine nucleotide and calmodulin and reflected a selective decrease in the apparent affinity of RYR1 activation sites for Ca ( 2+ ) relative to Mg ( 2+ )
Sun et al., Proc Natl Acad Sci U S A 2001 : Our results reveal that different cysteines within the channel have been adapted to serve in nitrosative and oxidative responses, and that S-nitrosylation of the cysteine containing CaM binding domain underlies the mechanism of CaM dependent regulation of RyR1 by NO
Rodney et al., Biochemistry 2001 : Calcium and calmodulin both regulate the skeletal muscle calcium release channel , also known as the ryanodine receptor, RYR1 ... Ca ( 2+ ) -free calmodulin ( apocalmodulin ) activates and Ca ( 2+ ) -calmodulin inhibits the ryanodine receptor
O'Connell et al., J Gen Physiol 2002 : The results indicate that CaM binding to the 3614-3643 region of RyR1 is not essential for voltage sensor activation of RyR1
Balog et al., J Biol Chem 2003 : Apo-CaM increases RyR1 channel activity, but Ca ( 2+ ) -CaM is inhibitory ... Here we examine the functional effects of CaM oxidation on RyR1 regulation by both apo-CaM and Ca ( 2+ ) -CaM, as assessed via determinations of [ ( 3 ) H ] ryanodine and [ ( 35 ) S ] CaM binding to skeletal muscle sarcoplasmic reticulum vesicles ... Mutating individual CaM Met residues to Gln demonstrated that Met-109 was required for apo-CaM activation of RyR1 but not for Ca ( 2+ ) -CaM inhibition of the channel
Fruen et al., Biochemistry 2003 : We conclude that Ca2+ binding to CaM determines the effect of CaM on both RYR1 and RYR2 channels and that isoform differences in CaM regulation reflect the differential tuning of Ca2+ binding sites on CaM when bound to the different RYRs
Yamaguchi et al., J Biol Chem 2003 : CaM inhibits the skeletal muscle ryanodine receptor ( RyR1 ) and cardiac muscle receptor ( RyR2 ) at >1 microm Ca2+ but activates RyR1 and inhibits RyR2 at <1 microm Ca2+ ... 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
Fruen et al., Biochemistry 2005 : Calmodulin (CaM) activates the skeletal muscle ryanodine receptor ( RyR1 ) at nanomolar Ca ( 2+ ) concentrations but inhibits it at micromolar Ca ( 2+ ) concentrations, indicating that binding of Ca ( 2+ ) to CaM may provide a molecular switch for modulating RyR1 channel activity
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
Guo et al., Circ Res 2006 : Ca2+/Calmodulin dependent protein kinase II phosphorylation of ryanodine receptor does affect calcium sparks in mouse ventricular myocytes
Boschek et al., Biochemistry 2007 (Ion Channel Gating) : Therefore, we have measured the calcium dependent activation of the individual domains of CaM in association with RyRp and their relationship to the CaM dependent regulation of RyR1
Boschek et al., Biochemistry 2008 : There is a biphasic regulation of RyR1 by unoxidized CaM , in which calcium activated CaM acts to enhance the calcium sensitivity of channel closure, while apo-CaM functions to enhance channel activity at resting calcium levels ... In contrast, the oxidation of CaM resulted in minimal functional changes in the CaM dependent activation of RyR1 at resting nanomolar calcium levels
Yamaguchi et al., Am J Physiol Cell Physiol 2011 : In vitro, calmodulin (CaM) and S100A1 activate the skeletal muscle ryanodine receptor ion channel ( RyR1 ) at submicromolar Ca ( 2+ ) concentrations, whereas at micromolar Ca ( 2+ ) concentrations, CaM inhibits RyR1 ... One amino acid substitution ( RyR1-L3625D ) has previously been demonstrated to impair CaM binding and regulation of RyR1
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
Lee et al., Nature 1994 : Cyclic ADP ribose activation of the ryanodine receptor is mediated by calmodulin
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
Zhang et al., Am J Physiol 1999 : CaM enhances the activity of RyR1 in low Ca2+ and inhibits its activity in high Ca2+