Enhancement of Ca2+ release channel activity by phosphorylation of the skeletal muscle ryanodine receptor

The Ca2+ 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...

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Bibliographic Details
Published in:FEBS letters 1993-10, Vol.332 (3), p.237-242
Main Authors: Herrmann-Frank, Annegret, Varsányi, Magdolna
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
Animals
Autoradiography
Ca2+ release
Ca2+-channel
Calcium - metabolism
Calcium Channels - isolation & purification
Calcium Channels - metabolism
Calcium Channels - physiology
Cell Membrane - metabolism
CHAPS, 3-[(3-cholamidopropyl)dimethylammonio]-1-propane-sulfonate
Lipid Bilayers - analysis
Lipid Bilayers - metabolism
Membrane Potentials
Muscle Proteins - isolation & purification
Muscle Proteins - metabolism
Muscle Proteins - physiology
Muscles - metabolism
P o, open probability
Pefabloc, 4-(2-aminoethyl)benzylsulfonylfluoride
Phosphoproteins - isolation & purification
Phosphoproteins - metabolism
Phosphorus Radioisotopes
Phosphorylation
PIPES, piperazine-N,N'-bis[2ethanesulfonic acid]
Rabbits
Ryanodine - metabolism
Ryanodine receptor
Ryanodine Receptor Calcium Release Channel
Sarcoplasmic reticulum
Sarcoplasmic Reticulum - metabolism
Skeletal muscle
SR, sarcoplasmic reticulum
T-tubule, transverse tubule, an infolded extension of the plasma membrane in close proximity to sarcoplasmic reticulum in muscle
Tritium
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Description
Summary:The Ca2+ 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 Ca2+ and ATP. The phosphorylation induced enhancement of the channel activity can be reversed by purified protein phosphatase 2A.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(93)80640-G