Key result
Cyclic AMP-dependent phosphorylation of phospholamban regulates the Ca2+ pump ATPase in the sarcoplasmic reticulum, modulating Ca2+ transients and the myocardial contractile response.
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Describes the fundamental molecular mechanism by which cAMP-dependent phosphorylation of phospholamban regulates the sarcoplasmic reticulum Ca2+ pump ATPase and myocardial contractility.
Ca2+ transients in myocardial cells are modulated by cyclic AMP-dependent phosphorylation of a protein in the sarcoplasmic reticulum. This protein, termed phospholamban, serves to regulate the Ca2+ pump ATPase of this membrane, thus altering the mode of Ca2+ transients and the myocardial contractile response. Elucidating the structure of phospholamban and its intimate interaction with the Ca2+ pump ATPase should provide the basis for understanding, at the molecular level, how the cAMP system contributes to excitation-contraction coupling in muscle cells.
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Tada et al. (1989) reported a review. Cyclic AMP-dependent phosphorylation of phospholamban regulates the Ca2+ pump ATPase in the sarcoplasmic reticulum, modulating Ca2+ transients and the myocardial contractile response.
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