The original, online version of this article contained a graphical abstract that was mislabeled, with the female somatic cells being labeled with AMH and the male cells being labeled with BMP2. The corrected graphical abstract, with the female somatic cells labeled with BMP2 and the male somatic cells labeled with AMH, is now included with both the online and print versions of our article. Both the erroneous and corrected graphical abstracts are also included below for the sake of comparison. We apologize for our initial mistake.

Dopamine is an important neurotransmitter in the central nervous system of both Drosophila and mammals. Despite the evolutionary distance, functional parallels exist between the fly and mammalian dopaminergic systems, with both playing roles in modulating locomotor activity, sexual function, and the response to drugs of abuse. In mammals, dopamine exerts its effects through either dopamine 1-like (D1-like) or D2-like G protein-coupled receptors. Although pharmacologic data suggest the presence of both receptor subtypes in insects, only cDNAs encoding D1-like proteins have been isolated previously. Here we report the cloning and characterization of a newly discovered Drosophila dopamine receptor. Sequence analysis reveals that this putative protein shares highest homology with known mammalian dopamine 2-like receptors. Eight isoforms of the Drosophila D2-like receptor (DD2R) transcript have been identified, each the result of alternative splicing. The encoded heptahelical receptors range in size from 461 to 606 aa, with variability in the length and sequence of the third intracellular loop. Pharmacologic assessment of three DD2R isoforms, DD2R-606, DD2R-506, and DD2R-461, revealed that among the endogenous biogenic amines, dopamine is most potent at each receptor. As established for mammalian D2-like receptors, stimulation of the Drosophila homologs with dopamine triggers pertussis toxin-sensitive Gi͞o-mediated signaling. The D2-like receptor agonist, bromocriptine, has nanomolar potency at DD2R-606, -506, and -461, whereas multiple D2-like receptor antagonists (as established with mammalian receptors) have markedly reduced if any affinity when assessed at the fly receptor isoforms. The isolation of cDNAs encoding Drosophila D2-like receptors extends the range of apparent parallels between the dopaminergic system in flies and mammals. Pharmacologic and genetic manipulation of the DD2Rs will provide the opportunity to better define the physiologic role of these proteins in vivo and further explore the utility of invertebrates as a model system for understanding dopaminergic function in higher organisms. Dopamine is an essential catecholamine in the central nervous system of both mammals (1) and Drosophila (2). In mammals, dopamine modulates neurologic, cardiovascular, endocrine, and renal functions. In addition, this neurotransmitter regulates motor activity, sexual behavior, and the response to drugs of abuse (1, 3-6). In Drosophila, known dopamine-mediated functions overlap with those of mammals. Experimental evidence suggests that in flies dopamine modulates locomotor activity, sexual function and the response to cocaine, nicotine, and alcohol (7-11).Dopaminergic signaling is mediated through seven transmembrane domain (TM) G protein-coupled receptors that fall within the class A or rhodopsin family based on amino acid homology and conservation of amino acid signature motifs. The dopamine receptor family is divided into two major subfamilies: the D1-like receptors (D1 and D5) and D2-like receptors (D2, D3, and ...

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