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Several G<jats:sub>s<\/jats:sub>-coupled receptors that couple to protein kinase A (PKA) readily recruit phosphorylation of GluR1 at S845. Conversely, activation of the ionotropic glutamate NMDA receptor (NMDAR) readily recruits dephosphorylation of the same GluR1 site through Ca<jats:sup>2+<\/jats:sup>-mediated recruitment of phosphatase activity. In a physiological setting, receptor activation often overlaps and crosstalk between coactivation of multiple signaling cascades can result in differential regulation of a given substrate. After investigating the effect of coactivation of the NMDAR and the G<jats:sub>s<\/jats:sub>-coupled \u03b2-adrenergic receptor on GluR1 phosphorylation state, we have observed a novel signal that prevents PKA-mediated phosphorylation of GluR1 at serine site 845. This blockade of GluR1 phosphorylation is dependent on cellular depolarization recruited by either NMDAR or AMPAR activation, independent of Ca<jats:sup>2+<\/jats:sup>and independent of calcineurin, protein phosphatase 1, and\/or protein phosphatase 2A activity. Thus, in addition to the typical kinase\u2013phosphatase rivalry mediating protein phosphorylation state, we have identified a novel form of phospho-protein regulation that occurs at GluR1 and may also occur at several other PKA substrates.<\/jats:p>","DOI":"10.1523\/jneurosci.3572-05.2006","type":"journal-article","created":{"date-parts":[[2006,1,25]],"date-time":"2006-01-25T20:28:04Z","timestamp":1138220884000},"page":"1138-1145","source":"Crossref","is-referenced-by-count":22,"title":["Novel Blockade of Protein Kinase A-Mediated Phosphorylation of AMPA Receptors"],"prefix":"10.1523","volume":"26","author":[{"given":"Amanda M.","family":"Vanhoose","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julie M.","family":"Clements","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danny 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