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Characterization of a tyramine receptor from Caenorhabditis elegans

Octopamine (OA) plays an important role in the regulation of a number of key processes in nematodes, including pharyngeal pumping, locomotion and egg‐laying. However, while putative OA receptors can be tentatively identified in the Caenorhabditis elegans database, no OA receptors have been functionally characterized from any nematode. We have isolated two cDNAs, ser‐2 and ser‐2a, encoding putative C.elegans serotonin/OA receptors (C02D4.2, ser‐2). The sequences of these cDNAs differ from that predicted by GeneFinder and lack 42 bp of exon 2. In addition, ser‐2a appears to be alternatively spliced and lacks a predicted 23 amino acids in the third intracellular loop. COS‐7 cells expressing SER‐2 bind [3H]LSD in the low nM range and exhibit Kis for tyramine, octopamine and serotonin of 0.07, 2, and 13.7 µm, respectively. Significantly, tyramine reduces forskolin‐stimulated cAMP levels in HEK293 cells stably expressing SER‐2 with an IC50 of about 360 nm, suggesting that SER‐2 is a tyramine receptor.