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The Journal of Neuroscience, June 15, 2000, 20(12):4480-4488
Regulation of Phosphorylation of the GluR1 AMPA Receptor in the Neostriatum by Dopamine and Psychostimulants In Vivo
Gretchen L. Snyder1, Patrick B. Allen1, Allen A. Fienberg1, Carmina G. Valle1, Richard L. Huganir2, Angus C. Nairn1, and Paul Greengard1 1 Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, New York, New York 10021, and 2 Department of Neuroscience, Howard Hughes Medical Institute, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
The activation of cAMP-dependent protein kinase regulates the physiological activity of AMPA-type glutamate receptors. In this study, phosphorylation of the AMPA receptor subunit GluR1 at Ser845 was increased in neostriatal slices by activation of D1-type dopamine receptors and by inhibitors of protein phosphatase 1/protein phosphatase 2A. In contrast, Ser831, a residue which, when phosphorylated by protein kinase C or calcium/calmodulin-dependent kinase II, increases AMPA receptor channel conductance, was unaffected by either D1 or D2 receptor agonists in neostriatal slices. The phosphorylation of Ser845, but not Ser831, was strongly increased in neostriatum in vivo in response to the psychostimulants cocaine and methamphetamine. The effects of dopamine and psychostimulants on the phosphorylation of GluR1 were attenuated in dopamine and cAMP-regulated phosphoprotein Mr 32 kDa (DARPP-32) knock-out mice. These results identify DARPP-32 and AMPA-type glutamate receptors as likely essential cellular effectors for psychostimulant actions.
Key words: dopamine; DARPP-32; methamphetamine; cocaine; protein phosphatase 1; D1 receptor; protein kinase A
Copyright © 2000 Society for Neuroscience 0270-6474/00/20124480-09$05.00/0
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