Functional properties of Drosophila dopamine D1-receptors are not altered by the size of the N-terminus.
Molecular cloning revealed the existence of at least five pharmacologically different dopamine receptors in vertebrates. Functionally, dopamine receptors either activate (D1-type), inhibit or do not interact with adenylate cyclase (D2-type). A recently cloned dopamine receptor from Drosophila melanogaster shares many structural and functional properties with vertebrate D1-type receptors but the pharmacological properties are very different. In contrast to most aminergic receptors, DmDop1 contains a long N-terminal extension. Here we describe a deletion-mutagenesis approach to study whether the N-terminus of DmDop1 participates in receptor-ligand interactions. All mutants gave rise to functional receptors after heterologous expression in HEK 293 cells. The pharmacological properties, however, remained unchanged. A comparison of DNA and deduced amino acid sequences revealed that some Drosophila strains express a truncated version of the DmDop1 receptor.
Gotzes
F
F
Institut für Biologische Informationsverarbeitung, Forschungszentrum Jülich, Germany.
Baumann
A
A
D000818:Animals; D001483:Base Sequence; D000242:Cyclic AMP / Q000378:metabolism; D017931:DNA Primers / Q000737:chemistry; D004331:Drosophila melanogaster; D008969:Molecular Sequence Data; D017447:Receptors, Dopamine D1 / Q000737:chemistry*; D016415:Sequence Alignment; D017384:Sequence Deletion; D012689:Sequence Homology, Nucleic Acid; D012995:Solubility; D013045:Species Specificity; D013329:Structure-Activity Relationship
D017931:DNA Primers; D017447:Receptors, Dopamine D1; D000242:Cyclic AMP