Abstract:
: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.
journal_name
Neuronjournal_title
Neuronauthors
Garcia EP,Mehta S,Blair LA,Wells DG,Shang J,Fukushima T,Fallon JR,Garner CC,Marshall Jdoi
10.1016/s0896-6273(00)80590-5subject
Has Abstractpub_date
1998-10-01 00:00:00pages
727-39issue
4eissn
0896-6273issn
1097-4199pii
S0896-6273(00)80590-5journal_volume
21pub_type
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