D(2)-Dopamine receptors target regulator of G protein signaling 9-2 to detergent-resistant membrane fractions.

Abstract

Detergent-resistant membranes (DRM) are thought to contain structures such as lipid rafts that are involved in compartmentalizing cell membranes. We report that the majority of D(2)-dopamine receptors (D(2)R) expressed endogenously in mouse striatum or expressed in immortalized cell-lines is found in DRM. In addition, exogenous co-expression of D(2)R in a cell line shifted the expression of regulator of G protein signaling 9-2 (RGS9-2) into DRM. RGS9-2 is a protein that is highly enriched in the striatum and specifically regulates striatal D(2)R. In the striatum, RGS9-2 is mostly associated with DRMs but when expressed in cell lines, RGS9-2 is present in the soluble cytoplasmic fraction. In contrast, the majority of mu opioid receptors and delta opioid receptors are found in detergent-soluble membrane and there was no shift of RGS9-2 into DRM after co-expression of mu opioid receptor. These data suggest that the targeting of RGS9-2 to DRM in the striatum is mediated by D(2)R and that DRM is involved in the formation of a D(2)R signaling complex. D(2)R-mediated targeting of RGS9-2 to DRM was blocked by the deletion of the RGS9-2 DEP domain or by a point mutation that abolishes the GTPase accelerating protein function of RGS9-2.

DOI: 10.1111/j.1471-4159.2011.07559.x

Cite this paper

@article{Celver2012D2DopamineRT, title={D(2)-Dopamine receptors target regulator of G protein signaling 9-2 to detergent-resistant membrane fractions.}, author={Jeremy P Celver and Meenakshi Sharma and Abraham Kovoor}, journal={Journal of neurochemistry}, year={2012}, volume={120 1}, pages={56-69} }