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Novel Interaction of the Dopamine D₂ Receptor and the Ca²⁺ Binding Protein S100B: Role in D₂ Receptor Function

Department of Behavioral Neuroscience, Oregon Health & Science University, Portland, Oregon (Y.L., D.C.B., K.A.N.); and Portland Veterans Affairs Medical Center, Portland, Oregon (D.C.B, K.A.N.)

S100B is a calcium-binding protein with both extracellular and intracellular regulatory activities in the mammalian brain. We have identified a novel interaction between S100B and the dopamine D₂ receptor. Our results also suggest that the binding of S100B to the dopamine D₂ receptor enhances receptor signaling. This conclusion is based on the following observations: 1) S100B and the third cytoplasmic loop of the dopamine D₂ receptor interact in a bacterial two-hybrid system and in a poly-histidine pull-down assay; 2) immunoprecipitation of the D₂ receptor also precipitates FLAG-S100B from human embryonic kidney 293 cell homogenates and endogenous S100B from rat neostriatal homogenates; 3) S100B immunoreactivity was detected in cultured neostriatal neurons expressing the D₂ receptor; 4) a putative S100B binding motif is located at residues 233 to 240 of the D₂ receptor, toward the amino terminus of the third cytoplasmic loop. D₃-IC3, which does not bind S100B, does not contain this motif; and 5) coexpression of S100B in D₂ receptor-expressing 293 cells selectively increased D₂ receptor stimulation of extracellular signal-regulated kinases and inhibition of adenylate cyclase.

Address correspondence to: Dr. Kim A. Neve, 3710 SW US Veterans Hospital Road, Portland, OR 97239-2999. E-mail: nevek{at}ohsu.edu

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