Gene interactions and pathways from curated databases and text-mining

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CALM1 — RYR2

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

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
Rodney et al., Biochemistry 2001 : Ca ( 2+ ) -free calmodulin ( apocalmodulin ) activates and Ca ( 2+ ) -calmodulin inhibits the ryanodine receptor
Hill et al., Mol Pharmacol 2004 : Functional regulation of the cardiac ryanodine receptor by suramin and calmodulin involves multiple binding sites
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
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
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
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