Cyclic AMP-dependent phosphorylation of a neuronal acetylcholine receptor alpha-type subunit
| Autor: | Stanley W. Halvorsen, Sukumar Vijayaraghavan, HA Schmid, Darwin K. Berg |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Agonist
medicine.medical_specialty medicine.drug_class Protein subunit 8-Bromo Cyclic Adenosine Monophosphate Chick Embryo Neurotransmission Biology Phosphates 1-Methyl-3-isobutylxanthine Internal medicine Cyclic AMP medicine Animals Receptors Cholinergic Phosphorylation Receptor Immunosorbent Techniques Acetylcholine receptor Neurons General Neuroscience Ciliary ganglion Ganglia Parasympathetic Articles Cell biology Kinetics Nicotinic agonist Endocrinology Electrophoresis Polyacrylamide Gel |
| Zdroj: | The Journal of Neuroscience. 10:3255-3262 |
| ISSN: | 1529-2401 0270-6474 |
| DOI: | 10.1523/jneurosci.10-10-03255.1990 |
| Popis: | Chick ciliary ganglion neurons have nicotinic acetylcholine receptors (AChRs) that mediate synaptic transmission through the ganglion. A cAMP- dependent process has previously been shown to enhance the ACh response of the neurons 2- to 3-fold without requiring the synthesis of new receptors. We show here that the receptors can be phosphorylated in situ by a cAMP-dependent process. The phosphorylation occurs predominantly on components of 50 and 58 kDa. Both derive from putative ligand-binding alpha 3 subunits, with the smaller phosphorylated species probably representing a degradation product of the larger. The increase in receptor phosphorylation caused by incubating the neurons with a cAMP analog parallels the increase observed in the ACh response, with respect to both time course and relative extent. The phosphorylation of ciliary ganglion AChRs differs from that reported for electric organ AChRs, which occurs primarily on the non-ligand- binding gamma and delta subunits and increases the rate of agonist- induced receptor desensitization. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|