The Multidimensional Partnership of EcR and USP

Henrich, Vincent C.; Beatty, Joshua; Ruff, Heike; Callender, Jenna L.; Grebe, Marco; Spindler-Barth, Margarethe

doi:10.1007/978-1-4020-9112-4_14

Cited by 12 publications

(15 citation statements)

References 51 publications

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“…Mutational analysis revealed that amino acids involved in phospholipid binding and amino acids considered as putative juvenile hormone binding sites are important for receptor function [43].…”

Section: Ligand Bindingmentioning

confidence: 99%

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Ecdysteroid hormone action

Spindler

Honl

Tremmel

et al. 2009

Cell. Mol. Life Sci.

103

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Several reviews devoted to various aspects of ecdysone research have been published during the last few years. Therefore, this article concentrates mainly on the considerable progress in ecdysone research observed recently, and will cover the results obtained during the last 2 years. The main emphasis is put on the molecular mode of ecdysteroid receptor-mediated hormone action. Two examples of interaction with other hormonal signalling pathways are described, namely crosstalk with juvenile hormone and insulin. Some selected, recently investigated examples of the multitude of hormonal responses are described. Finally, ecological aspects and some practical applications are discussed.

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Section: Ligand Bindingmentioning

confidence: 99%

“…Transcriptional activity of the ecdysteroid receptor Heterologeous expression of EcR and Usp in vertebrate cells is considered a suitable model to study transcriptional activity of the receptor complex [43]. Since vertebrate cells are devoid of endogenous EcR and some subclones of cell lines, e.g.…”

Section: Interaction Of the Receptor Complex With Dnamentioning

confidence: 99%

Ecdysteroid hormone action

Spindler

Honl

Tremmel

et al. 2009

Cell. Mol. Life Sci.

103

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“…We used CHO-K1 cells, which were routinely used for heterologous studies of the EcR/USP complex [26]. The rationale for using heterologous cell cultures to test EcR and USP function is discussed extensively by Henrich et al [27]. These studies will be the basis for an in vivo approach, which will allow the discrimination, which receptor property is used and how receptor activity is modulated to adapt ecdysteroid receptor function to the actual physiological requirements of different insect tissues during various developmental stages.…”

Section: Resultsmentioning

confidence: 99%

“…A heterologous cell culture system allows for direct comparisons of the ecdysteroid receptor-mediated transcriptional activity using a variety of individual promoters [27]. Because these studies are carried out in a cellular environment that is constant, using cells which display no endogenous ecdysteroid receptor activity, the capability exists to analyze and compare effects of EcR isoforms and modified USP constructs directly.…”

Section: Discussionmentioning

confidence: 99%

The N-terminus of ecdysteroid receptor isoforms and ultraspiracle interacts with different ecdysteroid response elements in a sequence specific manner to modulate transcriptional activity

Schauer

Callender

Henrich

et al. 2011

The Journal of Steroid Biochemistry and Molecular Biology

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“…To evaluate the potency of EcR isoforms, heterologous expression of receptor proteins was used successfully. Expression of EcR and Usp in vertebrate cells and yeast cells has the advantage that no endogenous receptors interfere with the hormone response (Henrich et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

DNA‐binding properties of Drosophila ecdysone receptor isoforms and their modification by the heterodimerization partner ultraspiracle

Braun

Azoitei

Spindler-Barth

2009

Arch Insect Biochem Physiol

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Transcriptional activity of ecdysone receptor (EcR) isoforms varies considerably and is modified further by the heterodimerization partner and hormone treatment. To investigate whether differences in DNA binding of receptor complexes are responsible for these variations in transcriptional activity, interaction of Drosophila EcR isoforms, and variants of Ultraspiracle (Usp), the orthologue of RXR, with the ecdysone response elements (EcRE) hsp 27, PAL-1, and DR-1, were determined by electrophoretic mobility shift assays. Receptor proteins were expressed in vertebrate cells (CHO-K1) in order to rule out an influence of endogenous receptor proteins. In the absence of a heterodimerization partner, weak DNA binding of EcR was detected even without hormone with EcR-A and -B1, but not EcR-B2. In the presence of hormone, all three isoforms show increased binding to the hsp 27 EcRE. The heterodimerization partner Usp increased DNA binding considerably. The hormone effect of heterodimers is more pronounced with both EcR-B isoforms compared to EcR-A. Two specific bands were obtained for EcR-A and B1 but only one band is visible with EcR-B2. Deletion of the C-domain of Usp still allows basal DNA binding of the heterodimer, but in contrast to full-length Usp, addition of hormone decreases the intensity of the retarded receptor band of all EcR isoforms and the EcREs hsp27 and DR-1 considerably, whereas interaction with the EcRE PAL-1 is only slightly affected. Synergistic effects on transcriptional activity are associated with the formation of different receptor DNA-complexes observed with 1xhsp27 and 3xhsp27. Comparison of DNA-binding properties of EcR isoforms and EcR/Usp heterodimers revealed that binding of receptor complexes to hsp 27 EcRE is dependent on the AB domain of EcR and the AB-, C-, and D-domains of the heterodimerization partner. Interaction with the hsp 27 EcRE correlates neither with ligand binding nor with transcriptional activity of the various receptor complexes. We, therefore, conclude that the different receptor functions are regulated separately, for example, by interaction with co-modulators or post-transcriptional modifications.

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The Multidimensional Partnership of EcR and USP

Cited by 12 publications

References 51 publications

Ecdysteroid hormone action

Ecdysteroid hormone action

The N-terminus of ecdysteroid receptor isoforms and ultraspiracle interacts with different ecdysteroid response elements in a sequence specific manner to modulate transcriptional activity

DNA‐binding properties of Drosophila ecdysone receptor isoforms and their modification by the heterodimerization partner ultraspiracle

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