Abstract

Dopamine receptors are members of the G protein-coupled receptor family and are important for a variety of functions in the central nervous system, including drug reward, learning, motor activity and neuropsychiatric disorders. It has now been shown that many G protein-coupled receptors can form dimers or higher order oligomers and that this phenomenon has relevance to receptor function. Dopamine receptors have also been shown to exist as homodimers (or higher order oligomers) in the cells. Furthermore, evidence for heterodimerization has recently been provided for dopamine D 1 and adenosine At receptors, as well as for dopamine D 2 and somatostatin SSTR 5 and dopamine D 2 and adenosine A 2 receptors. In this paper, we reviewed our recent findings on dopamine D 2 and D 3 receptors interaction, and we illustrated how D 2 /D 3 heterodimerization can modify the pharmacology of these receptors.

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