Abstract
Glutamate receptor (GluR) δ2 selectively expressed in cerebellar Purkinje cells plays a central role in cerebellar long-term depression (LTD), motor learning, and formation of parallel fiber synapses. By yeast two-hybrid screening, we identified members of the Shank family of scaffold proteins as major GluRδ2-interacting molecules. GluRδ2 bound directly to the PDZ domain of Shank proteins through an internal motif in the carboxyl-terminal putative cytoplasmic domain. Shank1 and Shank2 proteins as well as GluRδ2 proteins were localized in the dendritic spines of cultured Purkinje cells. Anti-GluRδ2 antibodies immunoprecipitated Shank1, Shank2, Homer, and metabotropic GluR1α proteins from the synaptosomal membrane fractions of cerebella. Furthermore, Shank2 interacted with GRIP1 in the cerebellum. These results suggest that through Shank1 and Shank2, GluRδ2 interacts with the metabotropic GluR1α, the AMPA-type GluR, and the inositol 1,4,5-trisphosphate receptor (IP 3R) that are essential for cerebellar LTD.
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