Journal
NEURON
Volume 47, Issue 6, Pages 845-857Publisher
CELL PRESS
DOI: 10.1016/j.neuron.2005.08.016
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Funding
- NIDCD NIH HHS [Z01 DC000003-17] Funding Source: Medline
- NINDS NIH HHS [R01 NS047700-06, R01 NS047700] Funding Source: Medline
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The NMDA receptor (NMDAR) is a component of excitatory synapses and a key participant in synaptic plasticity. We investigated the role of two domains in the C terminus of the NR2B subunit-the PDZ binding domain and the clathrin adaptor protein (AP-2) binding motif-in the synaptic localization of NMDA receptors. NR2B subunits lacking functional PDZ binding are excluded from the synapse. Mutations in the AP-2 binding motif, YEKL, significantly increase the number of synaptic receptors and allow the synaptic localization of NR2B subunits lacking PDZ binding. Peptides corresponding to YEKL increase the synaptic response within minutes. In contrast, the NR2A subunit localizes to the synapse in the absence of PDZ binding and is not altered by mutations in its motif corresponding to YEKL of NR2B. This study identifies a dynamic regulation of synaptic NR2B-containing NMDARs through PDZ protein-mediated stabilization and AP-2-mediated internalization that is modulated by phosphorylation by Fyn kinase.
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