A Regulatory Role for RIP140 in Nuclear Receptor Activation

Treuter, Eckardt; Albrektsen, Tatjana; Johansson, Lotta; Leers, Jörg; Gustafsson, Jan‐Åke

doi:10.1210/mend.12.6.0123

Cited by 179 publications

(145 citation statements)

References 74 publications

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“…We have provided evidence that BTG1 stimulates TRa1 and RARa transcriptional activity to a similar extent as reported for other coactivators (Monden et al, 1997;Treuter et al, 1998;Ko et al, 2000) and physically interacts with these receptors. As previously shown for PGC1a (Puigserver et al, 1998), we first observed that this interaction occurred in the absence and presence of the respective ligands of each receptor, leading us to study the possibility that, in the absence of ligands, binding of a corepressor molecule to nuclear receptors could impair their ability to interact with BTG1.…”

Section: Btg1 Is a Coactivator Of Positive Regulators Of Myoblast Difsupporting

confidence: 77%

Coactivation of nuclear receptors and myogenic factors induces the major BTG1 influence on muscle differentiation

et al. 2005

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The btg1 (B-cell translocation gene 1) gene coding sequence was isolated from a translocation break point in a case of B-cell chronic lymphocytic leukaemia. We have already shown that BTG1, considered as an antiproliferative protein, strongly stimulates myoblast differentiation. However, the mechanisms involved in this influence remained unknown. In cultured myoblasts, we found that BTG1 stimulates the transcriptional activity of nuclear receptors (T3 and all-trans retinoic acid receptors but not RXRa and PPARc), c-Jun and myogenic factors (CMD1, Myf5, myogenin). Immunoprecipitation experiments performed in cells or using in vitro-synthesized proteins and GST pull-down assays established that BTG1 directly interacts with T3 and all-trans retinoic acid receptors and with avian MyoD (CMD1). These interactions are mediated by the transactivation domain of each transcription factor and the A box and C-terminal part of BTG1. NCoR presence induces the ligand dependency of the interaction with nuclear receptors. Lastly, deletion of BTG1 interacting domains abrogates its ability to stimulate nuclear receptors and CMD1 activity, and its myogenic influence. In conclusion, BTG1 is a novel important coactivator involved in the regulation of myoblast differentiation. It not only stimulates the activity of myogenic factors, but also of nuclear receptors already known as positive myogenic regulators.

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Section: Btg1 Is a Coactivator Of Positive Regulators Of Myoblast Difsupporting

confidence: 77%

Coactivation of nuclear receptors and myogenic factors induces the major BTG1 influence on muscle differentiation

et al. 2005

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“…Northern hybridizations were performed as described previously (24). The RIP140 probe was a radiolabeled BglII/XhoI 1-kb fragment from plasmid pSG5-HAhRIP140 (22).…”

Section: Methodsmentioning

confidence: 99%

“…Expression and Reporter Constructs-The HA-tagged RIP140 expression vector in pSG5, pSG5-HAhRIP140, was kindly provided by Dr. Jan-Ake Gustafsson (Karolinska Institute, Sweden) (22). The reporter gene, containing tandem RAREs fused to the minimal herpes simplex virus-thymidine kinase promoter and luciferase (RARE-TK-Luc), has been described previously (41).…”

Section: Methodsmentioning

confidence: 99%

“…The coregulator RIP140 contains 10 LXXLL motifs and like a classic coactivator interacts preferentially with ligand-bound nuclear receptors (11). However, RIP140 inhibits the transactivation function of ligand-bound nuclear receptors in reporter assays (12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22). RIP140 is now recognized as one of the first proteins of a unique class of coregulators that are able to repress ligand-bound nuclear receptors (23).…”

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confidence: 99%

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Limiting Effects of RIP140 in Estrogen Signaling

White¹,

Yore

Deng

et al. 2005

Journal of Biological Chemistry

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The receptor interacting protein 140 (RIP140) belongs to a unique subclass of nuclear receptor coregulators with the ability to bind and repress the action of a number of agonist-bound hormone receptors. We have previously demonstrated that all-trans-retinoic acid (RA) induction of RIP140 constitutes a rate-limiting step in the regulation of retinoid receptor signaling. Here we demonstrate that RIP140 is also a limiting regulator of estrogen receptor signaling. Overexpression of RIP140 dose dependently inhibits estrogen-dependent reporter activity in human breast cancer cells. Furthermore, small interfering RNA to RIP140 enhances estrogen-dependent signaling. Our previous studies indicate that RIP140 is a direct target of RA. We report here that RA can abrogate estrogen-mediated cell cycle re-entry. In addition, RA treatment of estrogen-dependent breast cancer cells opposes estrogen receptor-dependent reporter activity, implying that a proportion of RA effects are anti-estrogenic. We provide evidence for a role for RIP140 in mediating anti-estrogenic effects of RA. RIP140 small interfering RNA blocks RA-mediated repression of estrogen receptor activity and provides a growth advantage to estrogen-dependent cells. Together these data implicate a regulatory role for RIP140 in mediating anti-estrogenic effects of RA in estrogendependent breast cancer cells and suggest that acute regulation of coregulator expression may be a general mechanism to integrate diverse hormone signals.

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“…Furthermore, targets the SLC39A6/SNAIL pathway by miR-192 to reduce tumor metastasis in human hepatocellular carcinoma (Lian et al 2016). Nuclear receptor interacting protein 1 (NRIP1) also known as RIP140 transcriptional coregulator is a nuclear protein that specifi cally interacts with the hormone-dependent activation domain AF2 of nuclear hormone receptors and modulates transcriptional activity of the estrogen receptor ESR1 and glucocorticoid receptor NR3C1 (Treuter et al 1998). NRIP1 is a positive regulator of the circadian clock genes expression and involved in the regulation of various oncogenic signaling pathways, participates in the development and progression of solid tumors (Lapierre et al 2015).…”

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confidence: 99%

Hypoxic regulation of the expression of genes encoded estrogen related proteins in U87 glioma cells: eff ect of IRE1 inhibition

et al. 2017

Endocrine Regulations

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Objective. Th e aim of the present study was to examine the eff ect of inhibition of endoplasmic reticulum stress signaling, mediated by IRE1 (inositol requiring enzyme 1), which is a central mediator of the unfolded protein response on the expression of genes encoded estrogen related proteins (NRIP1/RIP140, TRIM16/EBBP, ESRRA/NR3B1, FAM162A/E2IG5, PGRMC2/PMBP, and SLC39A6/LIV-1) and their hypoxic regulation in U87 glioma cells for evaluation of their possible signifi cance in the control of glioma cells proliferation.Methods. Th e expression of NRIP1, EBBP, ESRRA, E2IG5, PGRMC2, and SLC39A6 genes in U87 glioma cells, transfected by empty vector pcDNA3.1 (control) and cells without IRE1 signaling enzyme function (transfected by dnIRE1) upon hypoxia, was studied by a quantitative polymerase chain reaction.Results. Inhibition of both enzymatic activities (kinase and endoribonuclease) of IRE1 signaling enzyme function up-regulates the expression of EBBP, E2IG5, PGRMC2, and SLC39A6 genes is in U87 glioma cells in comparison with the control glioma cells, with more signifi cant changes for E2IG5 and PGRMC2 genes. At the same time, the expression of NRIP1 and ESRRA genes is strongly down-regulated in glioma cells upon inhibition of IRE1. We also showed that hypoxia increases the expression of E2IG5, PGRMC2, and EBBP genes and decreases NRIP1 and ESRRA genes expression in control glioma cells. Furthermore, the inhibition of IRE1 in U87 glioma cells decreases the eff ect of hypoxia on the expression of E2IG5 and PGRMC2 genes, eliminates hypoxic regulation of NRIP1 gene, and enhances the sensitivity of ESRRA gene to hypoxic condition. Furthermore, the expression of SLC39A6 gene is resistant to hypoxia in both the glioma cells with and without IRE1 signaling enzyme function. Conclusions.Results of this investigation demonstrate that inhibition of IRE1 signaling enzyme function aff ects the expression of NRIP1, EBBP, ESRRA, E2IG5, PGRMC2, and SLC39A6 genes in U87 glioma cells in gene specifi c manner and these changes possibly contribute to the suppression of the cell proliferation. Most of these genes are regulated by hypoxia and preferentially through IRE1 signaling pathway of endoplasmic reticulum stress.

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A Regulatory Role for RIP140 in Nuclear Receptor Activation

Cited by 179 publications

References 74 publications

Coactivation of nuclear receptors and myogenic factors induces the major BTG1 influence on muscle differentiation

Coactivation of nuclear receptors and myogenic factors induces the major BTG1 influence on muscle differentiation

Limiting Effects of RIP140 in Estrogen Signaling

Hypoxic regulation of the expression of genes encoded estrogen related proteins in U87 glioma cells: eff ect of IRE1 inhibition

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