Evidence for a phosphorylation‐induced conformational change in phospholamban from the effects of three proteases

FEBS Letters

Huggins, John P.¹  England, Paul J.¹ 

[1] Department of Cellular Pharmacology, Smith Kline and French Research Ltd, The Frythe, Welwyn, AL6 9AR, England

关键词: Phospholamban;    Sarcoplasmic reticulum;    cyclic AMP;    Phosphorylation;    Ca2+-ATPase;    (Cardiac muscle);   

DOI  :  10.1016/0014-5793(87)81236-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown