Glutamate receptors sensitive to alpha-amino-3-hydroxy-5-methyl-4-isoxazolpropionate (AMPA) are ligand-activated cation channels that mediate the fast component of excitatory postsynaptic currents in neurons of the central nervous system. These channels are assembled from 4 related subunits, GLUR-A to GLUR-D with the GLUR-B (GRIA2) subunit rendering the channel almost impermeable to Ca(2+) Hollmann et al., 1991 .
NCBI Summary:
Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. These receptors are heteromeric protein complexes with multiple subunits, each possessing transmembrane regions, and all arranged to form a ligand-gated ion channel. The classification of glutamate receptors is based on their activation by different pharmacologic agonists. The GRIA1 belongs to a family of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptors. Each of the members (GRIA1-4) include fip and flop isoforms generated by alternative RNA splicing resulting in a difference of 9 amino acids. The receptor subunits encoded by each isoform vary in their signal transduction properties. The isoform presented here is the flip isoform. AMPA-sensitive channels become impermeable to calcium by editing of mRNA in the coding region of the second transmembrane domain of glutamate receptor subunit. It involves a change of the base A in genomic DNA to the base G in mRNA. The GRIA2 subunit mRNA is completely edited in human brain.
General function
Receptor, Channel/transport protein
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Cellular localization
Plasma membrane
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Ovarian function
Unknown
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Expression regulated by
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Ovarian localization
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This gene was found in a rat ovarian cDNA library (Unigene)