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 thermolys...

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Bibliographic Details
Published in:FEBS letters 1987-06, Vol.217 (1), p.32-36
Main Authors: Huggins, John P., England, Paul J.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Ca 2+-ATPase
Ca2+-ATPase
Calcium-Binding Proteins - isolation & purification
Calcium-Binding Proteins - metabolism
Calcium-Transporting ATPases - metabolism
Cardiac muscle
cyclic AMP
Fundamental and applied biological sciences. Psychology
Guinea Pigs
Miscellaneous
myocardium
Myocardium - analysis
Papain - pharmacology
Phospholamban
Phosphorylation
Protein Conformation - drug effects
Protein Kinases - metabolism
Proteins
Sarcoplasmic reticulum
Sarcoplasmic Reticulum - metabolism
Thermolysin - pharmacology
Trypsin - pharmacology
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Summary: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 Ca 2+-ATPase pump.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(87)81236-X