Key result
Phosphorylation of phospholamban greatly reduced its sensitivity to digestion by trypsin and thermolysin, suggesting a phosphorylation-induced conformational change.
Population
Cardiac membrane protein phospholamban
Comparison
Phosphorylation with the catalytic subunit of… vs Unphosphorylated phospholamban
Design
Preclinical
Authors
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Mechanistic insight into phospholamban-SERCA regulation; hypothesis-generating for cardiac therapies, pending in vivo human validation.
Phosphorylation of phospholamban induces a conformational change, suggesting a mechanism for how it relieves inhibition of the sarcoplasmic reticulum Ca2+-ATPase pump.
Huggins et al. (1987) studied this question. Phosphorylation by catalytic subunit of cyclic AMP-dependent protein kinase vs. Unphosphorylated phospholamban was evaluated on Sensitivity of phospholamban to digestion by trypsin and thermolysin. Phosphorylation of phospholamban greatly reduced its sensitivity to digestion by trypsin and thermolysin, suggesting a phosphorylation-induced conformational change.
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