ArticleOncogene2002
Promyelocytic leukemia protein PML inhibits Nur77-mediated transcription through specific functional interactions.
Article in Oncogene, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
- Improving risk stratification for 2022 European LeukemiaNet favorable-risk patients with acute myeloid leukemia.Innovation (Cambridge (Mass.)) · 2024Article
- On the Prevalence and Roles of Proteins Undergoing Liquid-Liquid Phase Separation in the Biogenesis of PML-Bodies.Biomolecules · 2023Article
- International Union of Basic and Clinical Pharmacology CXIII: Nuclear Receptor Superfamily-Update 2023.Pharmacological reviews · 2023Review
- Promyelocytic leukemia protein targets MK2 to promote cytotoxicity.EMBO reports · 2021Article
- Inhibitory effect of PPARγ on NLRP3 inflammasome activation.Theranostics · 2021Article
- The nuclear receptor NR4A1 is regulated by SUMO modification to induce autophagic cell death.PloS one · 2020Article
- Role of the nucleus in apoptosis: signaling and execution.Cellular and molecular life sciences : CMLS · 2015Review
- The function, regulation and therapeutic implications of the tumor suppressor protein, PML.Cell & bioscience · 2015Review
- PML-mediated signaling and its role in cancer stem cells.Oncogene · 2014Review
- Loss of the promyelocytic leukemia protein in gastric cancer: implications for IP-10 expression and tumor-infiltrating lymphocytes.PloS one · 2011Article
- Article
- Signal-dependent regulation of transcription by histone deacetylase 7 involves recruitment to promyelocytic leukemia protein nuclear bodies.Molecular biology of the cell · 2008Article
- Article
- Structure and function of latency-associated nuclear antigen.Current topics in microbiology and immunology · 2007Review
- The promyelocytic leukemia protein functions as a negative regulator of IFN-gamma signaling.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- p53 and Nur77/TR3 - transcription factors that directly target mitochondria for cell death induction.Oncogene · 2006Review
- Retinoid X receptor regulates Nur77/TR3-dependent apoptosis [corrected] by modulating its nuclear export and mitochondrial targeting.Molecular and cellular biology · 2004Article
- PML colocalizes with and stabilizes the DNA damage response protein TopBP1.Molecular and cellular biology · 2003Article
- Mouse cytomegalovirus immediate-early protein 1 binds with host cell repressors to relieve suppressive effects on viral transcription and replication during lytic infection.Journal of virology · 2003Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The promyelocytic leukemia protein PML is a tumor and growth suppressor and plays an important role in a multiple pathways of apoptosis and regulation of cell cycle progression. Our previous studies and others also documented a role of PML in transcriptional regulation through its association with transcription coactivator CBP and transcription corepressor HDAC. Here, we showed that PML is a potent transcriptional repressor of Nur77, an orphan receptor and a member of the steroid receptor superfamily of proteins. We found that PML represses Nur77-mediated transactivation through a physical and functional interaction between the two proteins. PML interacts with Nur-77 in vitro in a GST-pull down assay and in vivo by coimmunoprecipitation assay. PML/Nur77 colocalized in vivo in a double immunofluorescent staining and confocal microscopic analysis. Our study further showed that the coiled-coil domain of PML interacts with the DNA-binding domain of Nur77 (amino acids 267-332). Electrophoretic mobility shift assay demonstrated that PML interferes with Nur77 DNA binding in a dose-dependent manner. This study indicates that PML interacts with the DNA-binding domain of Nur77 and represses transcription by preventing it from binding to the target promoter. This study supports a role of PML/Nur77 interaction in regulating cell growth and apoptosis.
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Registered trials
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.