Abstract
The PLB monomer inhibits the Ca2+ pump of cardiac sarcoplasmic reticulum (SERCA2a) by decreasing the apparent Ca2+ affinity of the enzyme. Here we addressed the molecular mechanism of enzyme inhibition using a PLB triple-mutant, N27A, N30C, L37A-PLB (PLB3), which is a potent gain-of-function PLB mutant that is cross-linkable to SERCA2a at Lys328. We observed that the protein-protein interaction between PLB3 and SERCA2a was strictly Ca2+-dependent and that several fold higher Ca2+ concentrations were required to both dissociate PLB3 from SERCA2a and to stimulate Ca2+-ATPase activity.
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