Modulation of nicotinic acetylcholine receptor turnover by tyrosine phosphorylation in rat myotubes

The muscle nicotinic acetylcholine receptor (AChR) turns over at different rates depending on stage of synaptogenesis and innervation. Tyrosine phosphorylation modulates desensitization, interaction with cytoskeleton and lateral mobility in the membrane of AChR. To determine whether tyrosine phospho...

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Bibliographic Details
Published in:Neuroscience letters 2001-11, Vol.313 (1), p.37-40
Main Authors: Sava, Anna, Barisone, Ilaria, Di Mauro, Debora, Fumagalli, Guido, Sala, Carlo
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Biotinylation
Bungarotoxins - metabolism
Bungarotoxins - pharmacology
Cells, Cultured
Cytoskeleton - metabolism
Enzyme Inhibitors - pharmacology
Fundamental and applied biological sciences. Psychology
Iodine Radioisotopes
Muscle Fibers, Skeletal - cytology
Muscle Fibers, Skeletal - metabolism
Myotubes
Neuromuscular junction
Neuromuscular Junction - metabolism
Nicotinic acetylcholine receptor
Pervanadate
Phosphorylation
Phosphotyrosine - metabolism
Protein Tyrosine Phosphatases - antagonists & inhibitors
Protein Tyrosine Phosphatases - metabolism
Radioligand Assay
Rats
Rats, Sprague-Dawley
Receptors, Nicotinic - metabolism
Striated muscle. Tendons
Turnover
Tyrosine - metabolism
Tyrosine phosphatases
Vanadates - pharmacology
Vertebrates: osteoarticular system, musculoskeletal system
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Summary:The muscle nicotinic acetylcholine receptor (AChR) turns over at different rates depending on stage of synaptogenesis and innervation. Tyrosine phosphorylation modulates desensitization, interaction with cytoskeleton and lateral mobility in the membrane of AChR. To determine whether tyrosine phosphorylation also modulates the turnover of AChR, myotubes in vitro were exposed to the tyrosine phosphatase inhibitor pervanadate. Our data indicate that a transient increase of phosphotyrosine levels stabilized a fraction of AChRs. The effects were limited to the non-ε subunit-containing AChRs already present in the membrane. Tyrosine phosphorylation of the receptor occurred on the β subunit, was transient and stable molecules were not selectively tyrosine phosphorylated. The data indicate that modulation of phosphotyrosine levels in muscle cells provides signals to control AChR metabolic stability.
ISSN:0304-3940
1872-7972
DOI:10.1016/S0304-3940(01)02244-3