Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution. Export

@article{citeulike:2047032, abstract = {G-protein coupled receptors (GPCRs) are ancient, ubiquitous sensors vital to environmental and physiological signaling throughout organismal life. With the publication of the Drosophila genome, numerous "orphan" GPCRs have become available for functional analysis. Here we characterize two groups of GPCRs predicted as receptors for peptides with a C-terminal amino acid sequence motif consisting of -PRXamide (PRXa). Assuming ligand-receptor coevolution, two alternative hypotheses were constructed and tested. The insect PRXa peptides are evolutionarily related to the vertebrate peptide neuromedin U (NMU), or are related to arginine vasopressin (AVP), both of which have PRXa motifs. Seven Drosophila GPCRs related to receptors for NMU and AVP were cloned and expressed in Xenopus oocytes for functional analysis. Four Drosophila GPCRs in the NMU group (CG14575 [corrected], CG8795, CG9918, CG8784) are activated by insect PRXa pyrokinins, (-FXPRXamide), Cap2b-like peptides (-FPRXamide), or ecdysis triggering hormones (-PRXamide). Three Drosophila GPCRs in the vasopressin receptor group respond to crustacean cardioactive peptide (CCAP), corazonin, or adipokinetic hormone (AKH), none of which are PRXa peptides. These findings support a theory of coevolution for NMU and Drosophila PRXa peptides and their respective receptors.}, address = {Department of Entomology, 5429 Boyce Hall, University of California, Riverside, CA 92521, USA.}, author = {Park, Y. and Kim, Y. J. and Adams, M. E.}, citeulike-article-id = {2047032}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.162276199}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/12177421}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=12177421}, day = {20}, doi = {10.1073/pnas.162276199}, issn = {0027-8424}, journal = {Proc Natl Acad Sci U S A}, keywords = {akh, ccap, corazonin, drosophile, gpcr}, month = {August}, number = {17}, pages = {11423--11428}, posted-at = {2009-06-19 15:46:57}, priority = {0}, title = {Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution.}, url = {http://dx.doi.org/10.1073/pnas.162276199}, volume = {99}, year = {2002} }

TY - JOUR ID - citeulike:2047032 L3 - citeulike-article-id:2047032 N2 - G-protein coupled receptors (GPCRs) are ancient, ubiquitous sensors vital to environmental and physiological signaling throughout organismal life. With the publication of the Drosophila genome, numerous "orphan" GPCRs have become available for functional analysis. Here we characterize two groups of GPCRs predicted as receptors for peptides with a C-terminal amino acid sequence motif consisting of -PRXamide (PRXa). Assuming ligand-receptor coevolution, two alternative hypotheses were constructed and tested. The insect PRXa peptides are evolutionarily related to the vertebrate peptide neuromedin U (NMU), or are related to arginine vasopressin (AVP), both of which have PRXa motifs. Seven Drosophila GPCRs related to receptors for NMU and AVP were cloned and expressed in Xenopus oocytes for functional analysis. Four Drosophila GPCRs in the NMU group (CG14575 [corrected], CG8795, CG9918, CG8784) are activated by insect PRXa pyrokinins, (-FXPRXamide), Cap2b-like peptides (-FPRXamide), or ecdysis triggering hormones (-PRXamide). Three Drosophila GPCRs in the vasopressin receptor group respond to crustacean cardioactive peptide (CCAP), corazonin, or adipokinetic hormone (AKH), none of which are PRXa peptides. These findings support a theory of coevolution for NMU and Drosophila PRXa peptides and their respective receptors. IS - 17 JF - Proc Natl Acad Sci U S A SN - 0027-8424 AD - Department of Entomology, 5429 Boyce Hall, University of California, Riverside, CA 92521, USA. EP - 11428 TI - Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution. VL - 99 SP - 11423 KW - akh KW - ccap KW - corazonin KW - drosophile KW - gpcr AU - Park, Y AU - Kim, YJ AU - Adams, ME PY - 2002/08/20/ UR - http://dx.doi.org/10.1073/pnas.162276199 ER -