p-GluR-1 Antibody (Ser 863): sc-12624

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Glutamate receptors mediate most excitatory neurotransmission in the brain and play an important role in neural plasticity, neural development and neurodegeneration. Ionotropic glutamate receptors are categorized into NMDA receptors and kainate/AMPA receptors, both of which contain glutamate-gated, cation-specific ion channels. Kainate/AMPA receptors are co-localized with NMDA receptors in many synapses and consist of seven structurally related subunits designated GluR-1 to -7. The kainate/AMPA receptors are primarily responsible for the fast excitatory neuro-transmission by glutamate, whereas the NMDA receptors are functionally characterized by a slow kinetic and a high permeability for Ca++ ions. The NMDA receptors consist of five subunits: four epsilion subunits (epsilon 1, 2, 3 and 4) and one zeta subunit. The zeta subunit is expressed throughout the brainstem whereas the four epsilon subunits display limited distribution. Serine 831 is specifically phosphorylated by CaM kinase II and is the major site of CaM kinase II phosphorylation on GluR-1. In addition, treatment of hippocampal slice preparations with phorbol esters and forskolin increase the phosphorylation of Serine 831 and 845, respectively, indicating that protein kinase C and protein kinase A phosphorylate these residues in hippocampal slices. GluR-1 phosphorylation is critical for synaptic plasticity, and that identical stimulation conditions recruit different signal-transduction pathways depending on synaptic history.