Ca2+/Calmodulin-Dependent Protein Kinase II Phosphorylation Regulates the Cardiac Ryanodine Receptor

By X. Wehrens, S. Lehnart, S. Reiken, A. Marks. Circulation Research, 2004

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Ryanodine receptors: structure, expression, molecular details, and function in calcium release. (2010, background): “Ser2814, however, appears to only be phosphorylated by CaMKII whereas Ser2030 is only phosphorylated by PKA (Wehrens et al. 2004; Xiao et al. 2006).”
Ischemia/Reperfusion (2016, neutral): “CaMK also acts to enable Ca2+ release from cardiac SR (835), thereby contributing to calcium overload in myocardial I/R.”
Cell Biology of Ischemia/Reperfusion Injury (2012, background): “Moreover, CaMK can also facilitate the release Ca2þ from the SR in the heart (Wehrens et al., 2004) and may, therefore, be responsible for the detrimental alterations in SR Ca2þ handling seen in cardiac I/R.”
Calmodulin kinase II inhibition protects against structural heart disease (2005, background): “CaMKII activity may affect the sarcoplasmic reticulum ryanodine receptor Ca 2+ release channel”
Resveratrol Ameliorates Aging-Related Metabolic Phenotypes by Inhibiting cAMP Phosphodiesterases (2012, neutral): “Upon activation of Epac, the ryanodine receptor 2 (Ryr2) is phosphorylated and facilitates the release of Ca2+ from the endoplasmic reticulum/ sarcoplasmic reticulum (ER/SR) (Wehrens et al., 2004).”
Simulation of the Undiseased Human Cardiac Ventricular Action Potential: Model Formulation and Experimental Validation (2011, methodology): “Wehrens et al.[96] with KN-93 in rabbit) should be performed in human ventricular myocytes to validate model predictions.”