Abstract
The δ2 glutamate receptor (GluRδ2) is considered a member of the ionotropic glutamate receptor family, although a specific ligand that activates the wild-type receptor has yet to be identified. GluRδ2 is enriched in the parallel fiber-Purkinje cell (PF-PC) synapse, but the precise physiological role of the receptor is still unclear. A naturally-occurring single point mutant in the third transmembrane domain of the receptor (A654T), named Lurcher (GluRδ2Lc), exhibits constitutive activity.Our previous preliminary results suggested that the δ2 glutamate receptor - Lurcher mutant is inhibited by direct interactions with phosphatidylinositol 4,5-bisphosphate (PIP2). Here we show that pre-incubation with wortmannin affects the activity of the receptor in a concentration-dependent manner, leading to an inhibition of the channel in the low micromolar range. This suggests that phosphatidylinositol 3-kinase (PI3K) could also be involved in the regulation of the δ2 glutamate receptor. We further investigate the involvement of phosphoinositides in the regulation of δ2 glutamate receptor using more specific PI3K and PI4K inhibitors as well as soluble stereoisomers of different phosphoinositides.
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