SAP90 Binds and Clusters Kainate Receptors Causing Incomplete Desensitization
作者： Elizabeth P Garcia , Sunil Mehta , Leslie A.C Blair , David G Wells , Jing Shang
DOI: 10.1016/S0896-6273(00)80590-5
关键词: Peptide sequence 、 Kainate receptor 、 Neuroscience 、 Electrophysiology 、 NMDA receptor 、 Receptor 、 Cell biology 、 Desensitization (medicine) 、 Colocalization 、 Biology
摘要: The mechanism of kainate receptor targeting and clustering is still unresolved. Here, we demonstrate that members the SAP90/PSD-95 family colocalize associate with receptors. SAP90 SAP102 coimmunoprecipitate both KA2 GluR6, but only SAP97 coimmunoprecipitates GluR6. Similar to NMDA receptors, GluR6 mediated by interaction its C-terminal amino acid sequence, ETMA, PDZ1 domain SAP90. In contrast, region binds to, clustered by, SH3 GK domains Finally, show coexpressed or GluR6/KA2 receptors alters function reducing desensitization. These studies suggest organization electrophysiological properties synaptic are modified association family.
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