S100A1 Protein Does Not Compete with Calmodulin for Ryanodine Receptor Binding but Structurally Alters the Ryanodine Receptor·Calmodulin Complex

S100A1 has been suggested as a therapeutic agent to enhance myocyte Ca2+ cycling in heart failure, but its molecular mode of action is poorly understood. Using FRET, we tested the hypothesis that S100A1 directly competes with calmodulin (CaM) for binding to intact, functional ryanodine receptors typ...

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Veröffentlicht in:	The Journal of biological chemistry 2016-07, Vol.291 (30), p.15896-15907
Hauptverfasser:	Rebbeck, Robyn T., Nitu, Florentin R., Rohde, David, Most, Patrick, Bers, Donald M., Thomas, David D., Cornea, Razvan L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Calcium - chemistry Calcium - metabolism calcium channel calmodulin (CaM) Calmodulin - chemistry Calmodulin - genetics Calmodulin - metabolism FKBP12.6 fluorescence lifetime fluorescence resonance energy transfer (FRET) Fluorescence Resonance Energy Transfer - methods Humans Molecular Biophysics Muscle, Skeletal - chemistry Muscle, Skeletal - metabolism Myocardium - chemistry Myocardium - metabolism Protein Binding Ryanodine Receptor Calcium Release Channel - chemistry Ryanodine Receptor Calcium Release Channel - metabolism S100 Proteins - chemistry S100 Proteins - genetics S100 Proteins - metabolism sarcoplasmic reticulum (SR) structure-function Swine
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