PMID: 7541972May 10, 1995Paper

Phosphorylation of the nicotinic acetylcholine receptor by protein tyrosine kinases

Annals of the New York Academy of Sciences
S L SwopeR L Huganir

Abstract

Most neurotransmitter receptors examined to date are either regulated by phosphorylation or contain consensus sequences for phosphorylation by protein kinases. The nicotinic acetylcholine receptor (AChR), which mediates depolarization at the neuromuscular junction, has served as a model for the study of the structure, function, and regulation of ligand-gated ion channels. The AChR is phosphorylated by protein kinase A, protein kinase C, and an unidentified protein tyrosine kinase. Tyrosine phosphorylation of the AChR is correlated with a modulation of the rate of receptor desensitization and is associated with AChR clustering. We showed that agrin, a neuronally derived extracellular matrix protein, induces AChR clustering and tyrosine phosphorylation. In addition, we identified two protein tyrosine kinases, Fyn and Fyk, that appear to be involved in the regulation of synaptic transmission at the neuromuscular junction by phosphorylating the AChR. The two kinases are highly expressed in Torpedo electric organ, a tissue enriched in synaptic components including the AChR. As demonstrated by coimmunoprecipitation, Fyn and Fyk associate with the AChR. Furthermore, the AChR is phosphorylated in Fyn and Fyk immunoprecipitates. We inve...Continue Reading

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Citations

Dec 13, 1996·The Journal of Biological Chemistry·C Fuhrer, Z W Hall
Jan 1, 1997·Annual Review of Cell and Developmental Biology·S M Thomas, J S Brugge
Sep 2, 2009·Nature Reviews. Drug Discovery·Antoine TalyJean-Pierre Changeux
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May 25, 2021·Cellular and Molecular Life Sciences : CMLS·Juan Facundo ChrestiaCecilia Bouzat

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