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Journal of Pharmacology And Experimental Therapeutics Fast Forward
First published on March 3, 2009; DOI: 10.1124/jpet.108.149542

0022-3565/09/3293-1117-1126$20.00
JPET 329:1117-1126, 2009
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NEUROPHARMACOLOGY

Activation of Group I Metabotropic Glutamate Receptors Increases Serine Phosphorylation of GluR1 {alpha}-Amino-3-hydroxy-5-methylisoxazole-4-propionic Acid Receptors in the Rat Dorsal Striatum

Sung Min Ahn, and Eun Sang Choe

Department of Biological Sciences, Pusan National University, Pusan, Korea

Protein phosphorylation is an important mechanism for the post-translational modulation of ionotropic glutamate receptors. In this study, we investigated the regulation of {alpha}-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor GluR1 subunit phosphorylation by the stimulation of group I metabotropic glutamate receptors (mGluRs) in the rat dorsal striatum in vivo. Stimulation of group I mGluRs was found to increase GluR1 phosphorylation of Ser831 and Ser845 in phospholipase C (PLC)-coupled Ca2+ cascades. Interactions of protein kinases activated by intracellular Ca2+ release downstream to PLC modulate the phosphorylation state of GluR1 on Ser831 and Ser845: phosphorylation of GluR1 on Ser831 is up-regulated by the protein kinase C and calcium-calmodulin-dependent protein kinase (CaMK)/c-Jun N-terminal kinase (JNK) pathways, whereas phosphorylation of GluR1 on Ser845 is up-regulated by the protein kinase A (PKA), PKA/ERK1/2, and PKA/JNK pathways. The phosphorylation state of GluR1 on Ser831 and Ser845 and the activity of protein kinases are further regulated by protein phosphatases. These data suggest that GluR1 phosphorylation of Ser831 and Ser845 via stimulation of group I mGluRs is regulated by the interactions of PLC-coupled protein kinases and protein phosphatases in the dorsal striatum.

Received for publication December 7, 2008
Accepted March 2, 2009.

Address correspondence to: Dr. Eun Sang Choe, Department of Biological Sciences, Pusan National University, 30 Jangjeon-dong, Kumjeong-gu, Pusan 609-735, Korea. E-mail: eschoe{at}pusan.ac.kr






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