Functional characterization of a neuropeptide F-like receptor from Drosophila melanogaster

Cited 75 time in scopus
Metadata Downloads
Title
Functional characterization of a neuropeptide F-like receptor from Drosophila melanogaster
Author(s)
G Feng; V Reale; H Chatwin; K Kennedy; R Venard; C Ericsson; Kweon Yu; P D Evans; L M Hall
Bibliographic Citation
European Journal of Neuroscience, vol. 18, no. 2, pp. 227-238
Publication Year
2003
Abstract
A cDNA clone encoding a seven-transmembrane domain, G-protein-coupled receptor (NPFR76F, also called GPCR60), has been isolated from Drosophila melanogaster. Deletion mapping showed that the gene encoding this receptor is located on the left arm of the third chromosome at position 76F. Northern blotting and whole mount in situ hybridization have shown that this receptor is expressed in a limited number of neurons in the central and peripheral nervous systems of embryos and adults. Analysis of the deduced amino acid sequence suggests that this receptor is related to vertebrate neuropeptide Y receptors. This Drosophila receptor shows 62-66% similarity and 32-34% identity to type 2 neuropeptide Y receptors cloned from a variety of vertebrate sources. Coexpression in Xenopus oocytes of NPFR76F with the promiscuous G-protein G α16 showed that this receptor is activated by the vertebrate neuropeptide Y family to produce inward currents due to the activation of an endogenous oocyte calcium-dependent chloride current. Maximum receptor activation was achieved with short, putative Drosophila neuropeptide F peptides (Drm-sNPF-1,2 and 2s). Neuropeptide F-like peptides in Drosophila have been implicated in a signalling system that modulates food response and social behaviour. The identification of this neuropeptide F-like receptor and its endogenous ligand by reverse pharmacology will facilitate genetic and behavioural studies of neuropeptide functions in Drosophila.
Keyword
Chromosome mappingG-protein-coupled receptorNeuropeptide FReceptor pharmacologyRNA expressionXenopus oocyte expression
ISSN
0953-816X
Publisher
Wiley
DOI
http://dx.doi.org/10.1046/j.1460-9568.2003.02719.x
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.