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D 2 ‐Dopamine receptors target regulator of G protein signaling 9‐2 to detergent‐resistant membrane fractions
Author(s) -
Celver Jeremy,
Sharma Meenakshi,
Kovoor Abraham
Publication year - 2012
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2011.07559.x
Subject(s) - regulator of g protein signaling , microbiology and biotechnology , receptor , striatum , g protein , chemistry , biology , gtpase activating protein , dopamine , signal transduction , biochemistry , endocrinology
J. Neurochem. (2012) 120 , 56–69. 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.