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J. Biol. Chem., Vol. 278, Issue 8, 6307-6313, February 21, 2003

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Protein Kinase C Associates Directly with the GluR4 -Amino-3-hydroxy-5-methyl-4-isoxazole Propionate Receptor Subunit
EFFECT ON RECEPTOR PHOSPHORYLATION^*

Susana Santos Correia^§, Carlos Bandeira Duarte^¶, Carlos José Faro^§, Euclides Vieira Pires^§, and Ana Luísa Carvalho^¶

From the  Center for Neuroscience and Cell Biology, the ^§ Department of Biochemistry, and the ^¶ Department of Zoology, University of Coimbra, 3004-517 Coimbra, Portugal

Ionotropic glutamate receptors mediate the majority of excitatory synaptic transmission in the brain and are thought to be involved in learning and memory formation. The activity of -amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA)-type glutamate receptors can be regulated by direct phosphorylation of their subunits, which affects the electrophysiological properties of the receptor, and the receptor association with numerous proteins that modulate membrane traffic and synaptic targeting of the receptor. In the present study we investigated the association of protein kinase C (PKC)  isoform with the GluR4 AMPA receptor subunit. PKC was co-immunoprecipitated with GluR4 AMPA receptor subunit in rat cerebellum and in cultured chick retina cell extracts, and immunocytochemistry experiments showed co-localization of GluR4 and PKC in cultured chick retinal neurons. Pull-down assays showed that native PKC binds the GluR4 C-terminal membrane-proximal region, and recombinant PKC was retained by GST-GluR4 C-terminal fusion protein, suggesting that the kinase binds directly to GluR4. Furthermore, GST-GluR4 C-terminal protein was phosphorylated on GluR4 Ser-482 by bound kinases, retained by the fusion protein, including PKC. The GluR4 C-terminal segment that interacts with PKC, which lacks the PKC phosphorylation sites, inhibited histone H1 phosphorylation by PKC, to the same extent as the PKC pseudosubstrate peptide 19-31, indicating that PKC bound to GluR4 preferentially phosphorylates GluR4 to the detriment of other substrates. Additionally, PKC expression in GluR4 transfected human embryonic kidney 293T cells increased the amount of plasma membrane-associated GluR4. Our results suggest that PKC binds directly to GluR4, thereby modulating the function of GluR4-containing AMPA receptors.

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