Metabotropic glutamate and dopamine receptors co‐regulate AMPA receptor activity through PKA in cultured chick retinal neurones: effect on GluR4 phosphorylation and surface expression

Glutamate receptor phosphorylation has been implicated in several forms of modulation of synaptic transmission. It has been reported that protein kinase A (PKA) can phosphorylate the α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazolepropionate (AMPA) receptor subunit GluR4 on Ser842, both in vitro and in vivo....

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Published in:Journal of neurochemistry 2004-08, Vol.90 (3), p.673-682
Main Authors: Gomes, André R., Cunha, Paulo, Nuriya, Mutsuo, Faro, Carlos J., Huganir, Richard L., Pires, Euclides V., Carvalho, Ana Luísa, Duarte, Carlos B.
Format: Article
Language:English
Subjects:
Adenylyl Cyclases - drug effects
Adenylyl Cyclases - metabolism
Amacrine Cells - cytology
Amacrine Cells - metabolism
AMPA receptors
Animals
Biological and medical sciences
Biotinylation
Calcium - metabolism
Cell Membrane - metabolism
Cells, Cultured
Chick Embryo
chick retina
Colforsin - pharmacology
Cyclic AMP-Dependent Protein Kinases - drug effects
Cyclic AMP-Dependent Protein Kinases - metabolism
Enzyme Activators - pharmacology
Enzyme Inhibitors - pharmacology
Eye and associated structures. Visual pathways and centers. Vision
Fundamental and applied biological sciences. Psychology
GluR4
metabotropic receptors
Neurons - cytology
Neurons - metabolism
Phosphorylation
protein kinase A
Protein Transport - drug effects
Protein Transport - physiology
Receptors, AMPA - metabolism
Receptors, Dopamine - metabolism
Receptors, Dopamine D1 - drug effects
Receptors, Dopamine D1 - metabolism
Receptors, Metabotropic Glutamate - metabolism
Retina - cytology
Retina - embryology
Retina - metabolism
surface expression
Vertebrates: nervous system and sense organs
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Summary:Glutamate receptor phosphorylation has been implicated in several forms of modulation of synaptic transmission. It has been reported that protein kinase A (PKA) can phosphorylate the α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazolepropionate (AMPA) receptor subunit GluR4 on Ser842, both in vitro and in vivo. Here, we studied the regulation of GluR4 phosphorylation and intracellular trafficking by PKA and by metabotropic receptors coupled to adenylyl cyclase (AC), in cultured chick retinal amacrine‐like neurones, which are enriched in GluR4. The regulation of AMPA receptor activity by PKA and by metabotropic AC‐coupled receptors was also investigated by measuring the [Ca2+]i response to kainate in Na+‐free medium. Stimulation of AC with forskolin (FSK), or using the selective agonist of dopamine D1 receptors (±)‐1‐phenyl‐2,3,4,5‐tetrahydro‐(1H)‐3‐benzazepine‐7,8‐diol (SKF38393), increased the [Ca2+]i response to kainate, GluR4 phosphorylation at Ser842 and GluR4 surface expression. Pre‐incubation of the cells with (2S,2′R,3′R)‐2‐(2′,3′‐dicarboxycyclopropyl)glycine (DCG‐IV), an agonist of group II metabotropic glutamate receptors (mGluR), which are coupled to inhibition of AC, inhibited the effect of FSK and of SKF38393 on AMPA receptor activity, GluR4 phosphorylation and expression at the plasma membrane. These results indicate that there is a functional cross‐talk between dopamine D1 receptors and group II mGluR in the regulation of GluR4 phosphorylation and AMPA receptor activity. Our data show that GluR4 phosphorylation at Ser842 by PKA, and its recruitment to the plasma membrane upon phosphorylation, is regulated by metabotropic receptors.
ISSN:0022-3042
1471-4159
DOI:10.1111/j.1471-4159.2004.02519.x