PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity.

Authors: Esteban, JA  Shi, SH  Wilson, C  Nuriya, M  Huganir, RL  Malinow, R 
Citation: Esteban JA, etal., Nat Neurosci. 2003 Feb;6(2):136-43.
Pubmed: (View Article at PubMed) PMID:12536214
DOI: Full-text: DOI:10.1038/nn997

The regulated incorporation of AMPA receptors into synapses is important for synaptic plasticity. Here we examine the role of protein kinase A (PKA) in this process. We found that PKA phosphorylation of the AMPA receptor subunits GluR4 and GluR1 directly controlled the synaptic incorporation of AMPA receptors in organotypic slices from rat hippocampus. Activity-driven PKA phosphorylation of GluR4 was necessary and sufficient to relieve a retention interaction and drive receptors into synapses. In contrast, PKA phosphorylation of GluR1 and the activity of calcium/calmodulin-dependent kinase II (CaMKII) were both necessary for receptor incorporation. Thus, PKA phosphorylation of AMPA receptor subunits contributes to diverse mechanisms underlying synaptic plasticity.

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CRRD ID: 8553676
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.