Document Detail


The ligand-binding domains of the three RXR-USP nuclear receptor types support distinct tissue and ligand specific hormonal responses in transgenic Drosophila.
MedLine Citation:
PMID:  19268446     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In insects, 20-hydroxyecdysone acts by binding on a heterodimer constituted by the ecdysone receptor (EcR) and Ultraspiracle (USP), the homolog to the vertebrate retinoid X receptor (RXR). Two types of USP have been characterized based on their structure and function, Mecopterida USP (Diptera/Lepidoptera USP), in particular the fruitfly Drosophila melanogaster USP (DmUSP) and non Mecopterida USP, exemplified by the beetle Tribolium castaneum USP (TcUSP) both showing structural differences from the vertebrate RXR. Here, by combining in vivo and organ culture observations in Drosophila transgenic animals, we show that ectopic expression of GAL4-DmUSP, GAL4-TcUSP or GAL4-HsRXR results in tissue- and ligand-dependent activities. In parallel, we show that neither juvenile hormone (JH) nor the related methyl farnesoate has an effect on GAL4-USP activation although JH induces the expression of a factor inhibiting the receptor transcriptional activity in the presence of EcR or RXR agonists. This study suggests that not only is USP important for hormonal regulation, via heterodimer formation, but that tissue-specific expression of cofactors may represent a higher level of control of this regulation. This in vivo approach should lead to a better understanding of the modes of action of USP and the identification of transcriptional cofactors essential for its function.
Authors:
Yannick Beck; Claude Delaporte; Dino Moras; Geoff Richards; Isabelle M L Billas
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-03-04
Journal Detail:
Title:  Developmental biology     Volume:  330     ISSN:  1095-564X     ISO Abbreviation:  Dev. Biol.     Publication Date:  2009 Jun 
Date Detail:
Created Date:  2009-05-18     Completed Date:  2009-06-18     Revised Date:  2011-11-10    
Medline Journal Info:
Nlm Unique ID:  0372762     Medline TA:  Dev Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1-11     Citation Subset:  IM    
Affiliation:
Institut de Génétique et de Biologie Moléculaire et Cellulaire, Département de Biologie et de Génomique Structurales, Illkirch, France.
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MeSH Terms
Descriptor/Qualifier:
Animals
Animals, Genetically Modified
Binding Sites
DNA-Binding Proteins / metabolism*
Dimerization
Drosophila melanogaster / genetics*,  metabolism*
Ecdysterone / pharmacology
Ligands
Models, Biological
Protein Structure, Tertiary
Receptors, Cytoplasmic and Nuclear / metabolism*
Receptors, Steroid / metabolism
Retinoid X Receptors / metabolism*
Transcription Factors / metabolism*
Tribolium / metabolism
Chemical
Reg. No./Substance:
0/DNA-Binding Proteins; 0/Ligands; 0/Receptors, Cytoplasmic and Nuclear; 0/Receptors, Steroid; 0/Retinoid X Receptors; 0/Transcription Factors; 0/ecdysone receptor; 0/ultraspiracle protein, Drosophila; 5289-74-7/Ecdysterone

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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