High level transactivation by the ecdysone receptor complex at the core recognition motif

Vögtli, Martin; Elke, Carsten; Imhof, Markus O.; Lezzi, Markus

doi:10.1093/nar/26.10.2407

Cited by 69 publications

(62 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…High stringency EMSAs were performed as described under "Experimental Procedures." the SAAB technique) by the related EcR⅐USP complex from Drosophila (38) and sequences shown to bind Mosquito EcR/ USP with high affinity (39,40).…”

Section: Discussionmentioning

confidence: 99%

Identification of the DNA Binding Specificity and Potential Target Genes for the Farnesoid X-activated Receptor

Laffitte¹,

Kast²,

Nguyen³

et al. 2000

Journal of Biological Chemistry

258

218

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Identification of the DNA Binding Specificity and Potential Target Genes for the Farnesoid X-activated Receptor

Laffitte¹,

Kast²,

Nguyen³

et al. 2000

Journal of Biological Chemistry

258

218

View full text Add to dashboard Cite

show abstract

“…Putative sites were filtered using the cutoff Patser score $8.0 (Hertz and Stormo 1999). The following sequences are known binding sites for ECR_USP Scholnick et al 1986;Riddihough and Pelham 1987;Cherbas et al 1991;Antoniewski et al 1993;Vogtli et al 1998;Petersen et al 2003): 59-GGTTGAA TGAATT-39, 59-CGGTCATTGGCCG-39, 59-AGTTCGAGGCACC-39, 59-GTTTCAGTGAAAG-39, 59-GGGTCAATAGCCG-39, 59-CGTTGA ATCAATG-39, 59-ATTTCTTTGAATT-39, 59-GGTTCAATGCACT-39, 59-GGGTTCATGCACT-39, and 59-AGTTCAGCGGCTG-39.…”

Section: Motif Analysismentioning

confidence: 99%

Genomic mapping of binding regions for the Ecdysone receptor protein complex

Gauhar¹,

Sun²,

Hua³

et al. 2009

Genome Res.

115

View full text Add to dashboard Cite

We determined the physical locations of the heterodimeric Ecdysone receptor/Ultraspiracle (ECR/USP) nuclear hormone receptor complex throughout the entire nonrepetitive genome of Drosophila melanogaster using a cell line (Kc167) that differentiates in response to 20-hydroxyecdysone (20-HE). 20-HE, the natural ligand of this complex, controls major aspects of insect development, including molting, metamorphosis, and reproduction. Direct gene targets of 20-HE signaling were identified by combining this physical binding-site profiling with gene expression profiling after treatment with 20-HE. We found 502 significant regions of ECR/USP binding throughout the genome. Only 42% of these regions are nearby genes that are 20-HE responsive in these cells. However, at least three quarters of the remaining ECR/USP regions are near 20-HE-regulated genes in other tissue and cell types during metamorphosis, suggesting that binding at many regulatory elements in the genome is largely noncell-type specific. The majority (21/26) of the early targets of 20-HE encode transcriptional regulatory factors. To determine whether any of these targets are required for the morphological differentiation of these cells, we used RNAi to reduce the expression of each of the 26 early genes. Accordingly, we found that three direct targets of ECR/USP-hairy, vrille, and Hr4 -are required for cellular differentiation in response to the hormone. Initial mutational analysis of vrille in vivo reveals that it is required for metamorphosis.

show abstract

“…The functional EcR is commonly considered as a heterodimer consisting of two proteins, EcR and USP, yet our results clearly demonstrated that AaEcR alone, without USP, can function as a transactivator in yeast, in agreement with results obtained from DmEcR (Dela Cruz & Mak 1997). In vitro transcribed DmEcR (Vogtli et al 1998) and AaEcR (S F Wang and A S Raikhel, unpublished data) are able to bind DNA without USP. It is also conceivable that the EcR homodimer is able to communicate with yeast basal transcription machinery independently of the ligand.…”

Section: Role Of Other Co-activators/co-repressors In the Ligand-depementioning

confidence: 99%

Requirement of co-factors for the ligand-mediated activity of the insect ecdysteroid receptor in yeast

Tran

Shaaban²,

Askari³

et al. 2001

Journal of Molecular Endocrinology

View full text Add to dashboard Cite

In insects, a steroid hormone 20-hydroxyecdysone has an important role in regulating critical events such as development and reproduction. The action of 20-hydroxyecdysone is mediated by its binding to the ecdysteroid receptor (EcR), which requires a heterodimeric partner, ultraspiracle protein (USP), a homologue of the retinoid X receptor (RXR). The EcR-USP heterodimer represents a functional receptor complex capable of initiating transcription of early genes. Our goal was to establish a ligand-dependent transactivation system in yeast utilizing an insect EcR-USP heterodimer. This has been achieved using mosquito Aedes aegypti AaEcR-USP. Expression of AaEcR alone, but not USP, resulted in constitutive transcription of the ecdysone reporter gene coupled with the Drosophila heat shock protein-27 ecdysone response elements. Removal of the N-terminal A/B domain of AaEcR abolished its constitutive transcription. Constitutive transcription was also eliminated in the presence of its heterodimeric partner, AaUSPa, AaUSPb or mammalian RXR. This suggests that the A/B domain is essential for the EcR ligand-independent transactivation and its interaction with the yeast transcription complex. A ligand-mediated transactivation of Aa( A/B)EcR-USP or Aa( A/B)EcR-RXR heterodimers in response to an ecdysteroid agonist RH-5992 was observed only in the presence of GRIP1, a mouse co-activator. In the presence of a co-repressor, SMRT, Aa( A/B)EcR-USP heterodimer exhibited a ligand-dependent repression activity. In addition, ligand-dependent transactivation systems for spruce budworm and fruit fly ecdysone receptors were also reported. This is the first report establishing the requirements of cofactors for a highly efficient ligand-dependent function of the insect EcR-USP in yeast. These findings open a way to study insect EcR-USP structure and function and to identify ligands that are specific for a certain group of insects, such as mosquitoes.

show abstract

High level transactivation by the ecdysone receptor complex at the core recognition motif

Cited by 69 publications

References 46 publications

Identification of the DNA Binding Specificity and Potential Target Genes for the Farnesoid X-activated Receptor

Identification of the DNA Binding Specificity and Potential Target Genes for the Farnesoid X-activated Receptor

Genomic mapping of binding regions for the Ecdysone receptor protein complex

Requirement of co-factors for the ligand-mediated activity of the insect ecdysteroid receptor in yeast

Contact Info

Product

Resources

About