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Vol. 57, Issue 3, 446-452, March 2000
Department of Pharmacology, University of California, Irvine,
California
Proteins that bind to G protein-coupled receptors have recently
been identified as regulators of receptor anchoring and signaling. In
this study, actin-binding protein 280 (ABP-280), a widely expressed cytoskeleton-associated protein that plays an important role in regulating cell morphology and motility, was found to associate with
the third cytoplasmic loop of dopamine D2 receptors. The specificity of this interaction was originally identified in a yeast
two-hybrid screen and confirmed by protein binding. The functional
significance of the D2 receptor-ABP-280 association was
evaluated in human melanoma cells lacking ABP-280. D2
receptor agonists were less potent in inhibiting forskolin-stimulated
cAMP production in these cells. Maximal inhibitory responses of
D2 receptor activation were also reduced. Further yeast
two-hybrid experiments showed that ABP-280 association is critically
dependent on the carboxyl domain of the D2 receptor third
cytoplasmic loop, where there is a potential serine phosphorylation
site (S358). Serine 358 was replaced with aspartic acid to mimic the
effects of receptor phosphorylation. This mutant (D2S358D)
displayed compromised binding to ABP-280 and coupling to adenylate
cyclase. PKC activation also generated D2 receptor
signaling attenuation, but only in ABP-containing cells, suggesting a
PKC regulatory role in D2-ABP association. A mechanism for
these results may be derived from a role of ABP-280 in the clustering
of D2 receptors, as determined by immunocytochemical
analysis in ABP-deficient and replete cells. Our results suggest a new
molecular mechanism of modulating D2 receptor signaling by
cytoskeletal protein interaction.
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