This basic science study reveals that cardiac phospholamban consists of two distinct proteolipids with specific kinase substrate functions.
Highlights distinct kinase regulation of cardiac phospholamban; leaves open isoform-specific roles in human disease.
Phosphorylation of phospholamban by either a cAMP-dependent or a calmodulin-dependent kinase stimulates the Ca2+ transporting activity of cardiac sarcoplasmic reticulum membranes. It has now been found that phospholamban consists of 2 distinct proteins; one is the specific substrate for the cAMP-dependent phosphorylation, and the other for the calmodulin-dependent kinase. In spite of functional diversity, the 2 polypeptides share a number of properties. Among them, the proteolipid character, Mr, resistance to trypsinization, and subunit composition.
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Chiesi et al. (1983) studied this question.
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