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Targeting of PKA to glutamate receptors through a MAGUK-AKAP complex.

Authors: Colledge, M  Dean, RA  Scott, GK  Langeberg, LK  Huganir, RL  Scott, JD 
Citation: Colledge M, etal., Neuron. 2000 Jul;27(1):107-19.
Pubmed: (View Article at PubMed) PMID:10939335

Compartmentalization of glutamate receptors with the signaling enzymes that regulate their activity supports synaptic transmission. Two classes of binding proteins organize these complexes: the MAGUK proteins that cluster glutamate receptors and AKAPs that anchor kinases and phosphatases. In this report, we demonstrate that glutamate receptors and PKA are recruited into a macromolecular signaling complex through direct interaction between the MAGUK proteins, PSD-95 and SAP97, and AKAP79/150. The SH3 and GK regions of the MAGUKs mediate binding to the AKAP. Cell-based studies indicate that phosphorylation of AMPA receptors is enhanced by a SAP97-AKAP79 complex that directs PKA to GluR1 via a PDZ domain interaction. As AMPA receptor phosphorylation is implicated in regulating synaptic plasticity, these data suggest that a MAGUK-AKAP complex may be centrally involved.

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RGD Object Information
RGD ID: 2313285
Created: 2009-09-16
Species: All species
Last Modified: 2009-09-16
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.