Protein phosphorylation of nicotinic acetylcholine receptors.

Research output: Contribution to journalArticle

Abstract

The nicotinic acetylcholine receptor (nAcChR) is a ligand-gated ion channel found in the postsynaptic membranes of electric organs, at the neuromuscular junction, and at nicotinic cholinergic synapses of the mammalian central and peripheral nervous system. The nAcChR from Torpedo electric organ and mammalian muscle is the most well-characterized neurotransmitter receptor in biology. It has been shown to be comprised of five homologous (two identicle) protein subunits (alpha 2 beta gamma delta) that form both the ion channel and the neurotransmitter receptor. The nAcChR has been purified and reconstituted into lipid vesicles with retention of ion channel function and the primary structure of all four protein subunits has been determined. Protein phosphorylation is a major posttranslational modification known to regulate protein function. The Torpedo nAcChR was first shown to be regulated by phosphorylation by the discovery that postsynaptic membranes contain protein kinases that phosphorylate the nAcChR. Phosphorylation of the nAcChR has since been shown to be regulated by the cAMP-dependent protein kinase, protein kinase C, and a tyrosine-specific protein kinase. Phosphorylation of the nAcChR by cAMP-dependent protein kinase has been shown to increase the rate of nAcChR desensitization, the process by which the nAcChR becomes inactivated in the continued presence of agonist. In cultured muscle cells, phosphorylation of the nAcChR has been shown to be regulated by cAMP-dependent protein kinase, a Ca2+-sensitive protein kinase, and a tyrosine-specific protein kinase. Stimulation of the cAMP-dependent protein kinase in muscle also increases the rate of nAcChR desensitization and correlates well with the increase in nAcChR phosphorylation. The AcChR represents a model system for how receptors and ion channels are regulated by second messengers and protein phosphorylation.

Original languageEnglish (US)
Pages (from-to)183-215
Number of pages33
JournalCritical Reviews in Biochemistry and Molecular Biology
Volume24
Issue number3
StatePublished - 1989
Externally publishedYes

Fingerprint

Phosphorylation
Nicotinic Receptors
Proteins
Cyclic AMP-Dependent Protein Kinases
Ion Channels
Electric Organ
Muscle
Torpedo
Neurotransmitter Receptor
Protein Subunits
Protein-Tyrosine Kinases
Protein Kinases
Ligand-Gated Ion Channels
Membranes
Muscles
Neuromuscular Junction
Peripheral Nervous System
Neurology
Second Messenger Systems
Post Translational Protein Processing

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Protein phosphorylation of nicotinic acetylcholine receptors. / Huganir, Richard L; Miles, K.

In: Critical Reviews in Biochemistry and Molecular Biology, Vol. 24, No. 3, 1989, p. 183-215.

Research output: Contribution to journalArticle

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