ArticleMolecular endocrinology (Baltimore, Md.)2006
Receptor-interacting protein 140 is a repressor of the androgen receptor activity.
Article in Molecular endocrinology (Baltimore, Md.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 46 citations in OpenAlex.
- The role of microrna-346 in prostate cancer progression: Clinical significance and biomarker potential.Journal of medical biochemistry · 2025Article
- The transcription factor RIP140 regulates interferon γ signaling in breast cancer.International journal of cancer · 2025Article
- The Transcription Coregulator RIP140 Inhibits Cancer Cell Proliferation by Targeting the Pentose Phosphate Pathway.International journal of molecular sciences · 2022Article
- Effects of endurance training on metabolic enzyme activity and transporter protein levels in the skeletal muscles of orchiectomized mice.The journal of physiological sciences : JPS · 2022Article
- RIP140 inhibits glycolysis-dependent proliferation of breast cancer cells by regulating GLUT3 expression through transcriptional crosstalk between hypoxia induced factor and p53.Cellular and molecular life sciences : CMLS · 2022Article
- Review
- Investigation of RIP140 and LCoR as independent markers for poor prognosis in cervical cancer.Oncotarget · 2017Article
- Complex regulation of LCoR signaling in breast cancer cells.Oncogene · 2017Article
- Article
- Systematic evaluation of underlying defects in DNA repair as an approach to case-only assessment of familial prostate cancer.Oncotarget · 2015Article
- Downregulation of RIP140 in hepatocellular carcinoma promoted the growth and migration of the cancer cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015Article
- Nutrient Sensing via mTOR in T Cells Maintains a Tolerogenic Microenvironment.Frontiers in immunology · 2014Review
- Negative regulation of estrogen signaling by ERβ and RIP140 in ovarian cancer cells.Molecular endocrinology (Baltimore, Md.) · 2013Article
- The RIP140 gene is a transcriptional target of E2F1.PloS one · 2012Article
- Role of nuclear receptor corepressor RIP140 in metabolic syndrome.Biochimica et biophysica acta · 2011Review
- Stearoyl CoA desaturase (SCD) facilitates proliferation of prostate cancer cells through enhancement of androgen receptor transactivation.Molecules and cells · 2011Article
- Differential alterations in gene expression profiles contribute to time-dependent effects of nandrolone to prevent denervation atrophy.BMC genomics · 2010Article
- The transcriptional coregulator RIP140 represses E2F1 activity and discriminates breast cancer subtypes.Clinical cancer research : an official journal of the American Association for Cancer Research · 2010Article
- 14-3-3{eta} Amplifies Androgen Receptor Actions in Prostate Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2009Article
- Retinoic acid mediates long-paced oscillations in retinoid receptor activity: evidence for a potential role for RIP140.PloS one · 2009Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The androgen receptor (AR) is a ligand-activated transcription factor that controls growth and survival of prostate cancer cells. In the present study, we investigated the regulation of AR activity by the receptor-interacting protein 140 (RIP140). We first showed that RIP140 could be coimmunoprecipitated with the receptor when coexpressed in 293T cells. This interaction appeared physiologically relevant because chromatin immunoprecipitation assays revealed that, under R1881 treatment, RIP140 could be recruited to the prostate-specific antigen encoding gene in LNCaP cells. In vitro glutathione S-transferase pull-down assays provided evidence that the carboxy-terminal domain of AR could interact with different regions of RIP140. By means of fluorescent proteins, we demonstrated that ligand-activated AR was not only able to translocate to the nucleus but also to relocate RIP140 from very structured nuclear foci to a diffuse pattern. Overexpression of RIP140 strongly repressed AR-dependent transactivation by preferentially targeting the ligand binding domain-dependent activity. Moreover, disruption of RIP140 expression induced AR overactivation, thus revealing RIP140 as a strong AR repressor. We analyzed its mechanism of transrepression and first demonstrated that different regions of RIP140 could mediate AR-dependent repression. We then showed that the carboxy-terminal end of RIP140 could reverse transcriptional intermediary factor 2-dependent overactivation of AR. The use of mutants of RIP140 allowed us to suggest that C-terminal binding protein played no role in RIP140-dependent inhibition of AR activity, whereas histone deacetylases partly regulated that transrepression. Finally, we provided evidence for a stimulation of RIP140 mRNA expression in LNCaP cells under androgen treatment, further emphasizing the role of RIP140 in androgen signaling.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.