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Full-Text Articles in Life Sciences
Phosphorylation State-Dependent Interaction Between Akap7Δ/Γ And Phospholamban Increases Phospholamban Phosphorylation., Marc Rigatti, Andrew V. Le, Claire Gerber, Ion I. Moraru, Kimberly L. Dodge-Kafka
Phosphorylation State-Dependent Interaction Between Akap7Δ/Γ And Phospholamban Increases Phospholamban Phosphorylation., Marc Rigatti, Andrew V. Le, Claire Gerber, Ion I. Moraru, Kimberly L. Dodge-Kafka
UCHC Articles - Research
Changes in heart rate and contractility in response to sympathetic stimulation occur via activation of cAMP dependent protein kinase A (PKA), leading to phosphorylation of numerous substrates that alter Ca2+ cycling. Phosphorylation of these substrates is coordinated by A-kinase anchoring proteins (AKAPs), which recruit PKA to specific substrates [1]. Phosphorylation of the PKA substrate phospholamban (PLB) is a critical determinant of Ca2+ re-entry into the sarcoplasmic reticulum and is coordinated by AKAP7δ/γ [2,3]. Here, we further these findings by showing that phosphorylation of PLB requires interaction with AKAP7δ/γ and that this interaction …