Evidence for a phosphorylation-induced conformational change in phospholamban from the effects of three proteases.
The effect of the proteases trypsin, thermolysin and papain on the cardiac membrane protein phospholamban was examined before or after phosphorylating the protein with the catalytic subunit of cyclic AMP-dependent protein kinase. The sensitivity of phospholamban to digestion by trypsin and thermolysin was greatly reduced by phosphorylation, suggesting that phospholamban undergoes a conformational change upon phosphorylation. It is suggested that this change in conformation is the mechanism by which phospholamban phosphorylation relieves its inhibition of the sarcoplasmic reticulum Ca2+-ATPase pump.
D000818:Animals; D002135:Calcium-Binding Proteins / Q000302:isolation & purification / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D006168:Guinea Pigs; D009206:Myocardium / Q000032:analysis; D010206:Papain / Q000494:pharmacology*; D010766:Phosphorylation; D011487:Protein Conformation / Q000187:drug effects; D011494:Protein Kinases / Q000378:metabolism; D012519:Sarcoplasmic Reticulum / Q000378:metabolism; D013820:Thermolysin / Q000494:pharmacology*; D014357:Trypsin / Q000494:pharmacology*; D000099211:Phospholamban
D002135:Calcium-Binding Proteins; D000252:Calcium-Transporting ATPases; D010206:Papain; D011494:Protein Kinases; D013820:Thermolysin; D014357:Trypsin; D000099211:Phospholamban