SAP90 Binds and Clusters Kainate Receptors Causing Incomplete Desensitization

The mechanism of kainate receptor targeting and clustering is still unresolved. Here, we demonstrate that members of the SAP90/PSD-95 family colocalize and associate with kainate receptors. SAP90 and SAP102 coimmunoprecipitate with both KA2 and GluR6, but only SAP97 coimmunoprecipitates with GluR6....

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Bibliographic Details
Published in:Neuron (Cambridge, Mass.) Mass.), 1998-10, Vol.21 (4), p.727-739
Main Authors: Garcia, Elizabeth P, Mehta, Sunil, Blair, Leslie A.C, Wells, David G, Shang, Jing, Fukushima, Teruyuki, Fallon, Justin R, Garner, Craig C, Marshall, John
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Cell Line
COS Cells
GluK2 Kainate Receptor
Hippocampus - cytology
Hippocampus - metabolism
Humans
kainic acid receptors
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Neurons - metabolism
postsynaptic density 95 protein
Rats
Receptor Aggregation - physiology
Receptors, Kainic Acid - metabolism
SAP90 protein
SAP90-PSD95 Associated Proteins
Tissue Distribution
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Summary:The mechanism of kainate receptor targeting and clustering is still unresolved. Here, we demonstrate that members of the SAP90/PSD-95 family colocalize and associate with kainate receptors. SAP90 and SAP102 coimmunoprecipitate with both KA2 and GluR6, but only SAP97 coimmunoprecipitates with GluR6. Similar to NMDA receptors, GluR6 clustering is mediated by the interaction of its C-terminal amino acid sequence, ETMA, with the PDZ1 domain of SAP90. In contrast, the KA2 C-terminal region binds to, and is clustered by, the SH3 and GK domains of SAP90. Finally, we show that SAP90 coexpressed with GluR6 or GluR6/KA2 receptors alters receptor function by reducing desensitization. These studies suggest that the organization and electrophysiological properties of synaptic kainate receptors are modified by association with members of the SAP90/PSD-95 family.
ISSN:0896-6273
1097-4199
DOI:10.1016/S0896-6273(00)80590-5