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Enhancement of Ca 2+ release channel activity by phosphorylation of the skeletal muscle ryanodine receptor
Author(s) -
Herrmann-Frank Annegret,
Varsányi Magdolna
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80640-g
Subject(s) - chaps , phosphorylation , chemistry , ryanodine receptor , endoplasmic reticulum , phosphatase , skeletal muscle , protein kinase a , biophysics , biochemistry , adenosine triphosphate , membrane , biology , endocrinology
The Ca 2+ release channel of rabbit skeletal muscle sarcoplasmic reticulum (SR) can be phosphorylated by membrane associated protein kinase(s) utilizing endogenously synthesized or exogenously added ATP. The channel protein has been enriched in non‐phosphorylated and phosphorylated form from heavy SR following solubilization with CHAPS (3‐[(3‐cholamidopropyl)dimethylammonio‐1‐propane‐sulfonate) and ultracentrifugation on a linear sucrose/CHAPS gradient. Reconstitution of the isolated channels into planar bilayers shows that phosphorylation enhances the open probability by increasing the sensitivity towards micromolar Ca 2+ and ATP. The phosphorylation induced enhancement of the channel activity can be reversed by purified protein phosphatase 2A.