PubMed Journals: Nature

  Source:		PMID: 8094892

    		Nature. 1993 Feb 18;361(6413):637-41.
			Phosphorylation and modulation of recombinant
			GluR6 glutamate receptors by cAMP-dependent
			protein kinase.

			Raymond LA(1), Blackstone CD, Huganir RL.

			Author Information
			(1) Department of Neuroscience,
			Johns Hopkins University School of Medicine,
			Baltimore, Maryland 21205.

			Glutamate-gated ion channels mediate most
			excitatory synaptic transmission in the
			central nervous system and play crucial
			roles in synaptic plasticity, neuronal development
			and some neuropathological conditions. These
			ionotropic glutamate receptors have been
			classified according to their preferred
			agonists as NMDA (N-methyl-D-aspartate),
			AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole
			propionate) and KA (kainate) receptors.
			On the basis of sequence similarity and
			pharmacological properties, the recently
			cloned glutamate receptor subunits have
			been assigned as components of NMDA (NMDAR1,
			2A-D), AMPA (GluR1-4) and KA (GluR5-7, KA1,
			KA2) receptors. Protein phosphorylation
			of glutamate receptors by protein kinase
			C and cyclic AMP-dependent protein kinase
			(PKA) has been suggested to regulate their
			function, possibly playing a prominent role
			in certain forms of synaptic plasticity
			such as long-term potentiation and long-term
			depression. Here we report that the GluR6
			glutamate receptor, transiently expressed
			in mammalian cells, is directly phosphorylated
			by PKA, and that intracellularly applied
			PKA increases the amplitude of the glutamate
			response. Site-specific mutagenesis of the
			serine residue (Ser 684) representing a
			PKA consensus site completely eliminates
			PKA-mediated phosphorylation of this site
			as well as the potentiation of the glutamate
			response. These results provide evidence
			that direct phosphorylation of glutamate
			receptors modulates their function.

			DOI: 10.1038/361637a0 PMID: 8094892 [Indexed
			for MEDLINE]

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