ArticleLeukemia2011
The self-association coiled-coil domain of PML is sufficient for the oncogenic conversion of the retinoic acid receptor (RAR) alpha.
Article in Leukemia, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
20 citing papers in PubMed, 37 citations in OpenAlex.
- PML-driven sumoylation of PML::RARA-bound repressors drives hematopoietic progenitor immortalization.The Journal of experimental medicine · 2026Article
- Mutation in the UnrearrangedResearch (Washington, D.C.) · 2025Article
- Acute Promyelocytic Leukemia, Retinoic Acid, and Arsenic: A Tale of Dualities.Cold Spring Harbor perspectives in medicine · 2024Review
- History of Developing Acute Promyelocytic Leukemia Treatment and Role of Promyelocytic Leukemia Bodies.Cancers · 2024Review
- PML Body Biogenesis: A Delicate Balance of Interactions.International journal of molecular sciences · 2023Review
- AKT inhibitor Hu7691 induces differentiation of neuroblastoma cells.Acta pharmaceutica Sinica. B · 2023Article
- Stabilization of CCDC102B by Loss of RACK1 Through the CMA Pathway Promotes Breast Cancer MetastasisFrontiers in oncology · 2022Article
- PML nuclear body biogenesis and oligomerization-driven leukemogenesis.Blood science (Baltimore, Md.) · 2020Review
- B1 oligomerization regulates PML nuclear body biogenesis and leukemogenesis.Nature communications · 2019Article
- Acute Promyelocytic Leukemia: A History over 60 Years-From the Most Malignant to the most Curable Form of Acute Leukemia.Oncology and therapy · 2019Review
- Article
- Pml nuclear body disruption cooperates in APL pathogenesis and impairs DNA damage repair pathways in mice.Blood · 2018Article
- Differentiation therapy revisited.Nature reviews. Cancer · 2018Review
- p53 as an Effector or Inhibitor of Therapy Response.Cold Spring Harbor perspectives in medicine · 2015Review
- Transcription and methylation analyses of preleukemic promyelocytes indicate a dual role for PML/RARA in leukemia initiation.Haematologica · 2015Article
- The PML domain of PML-RARα blocks senescence to promote leukemia.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Interaction with RXR is necessary for NPM-RAR-induced myeloid differentiation blockade.Leukemia research · 2013Article
- Is PML a Tumor Suppressor?Frontiers in oncology · 2013Article
- Crystal structure of the Marburg virus GP2 core domain in its postfusion conformation.Biochemistry · 2012Article
- The cell biology of disease: Acute promyelocytic leukemia, arsenic, and PML bodies.The Journal of cell biology · 2012Review
Corrections and comments
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Authors and funding
16 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In acute promyelocytic leukemia (APL) the retinoic acid receptor alpha (RARα) becomes an oncogene through the fusion with several partners, mostly with promyelocytic leukemia protein (PML), all of which have in common the presence of a self-association domain. The new fusion proteins, therefore, differently from the wild-type RARα, which forms only heterodimers with retinoic X receptor alpha, are also able to homo-oligomerize. The presence of such a domain has been suggested to be crucial for the leukemogenic potential of the chimeric proteins found in APL blasts. Whether or not any self-association domain is sufficient to bestow a leukemogenic activity on RARα is still under investigation. In this work, we address this question using two different X-RARα chimeras, where X represents the coiled-coil domain of PML (CC-RARα) or the oligomerization portion of the yeast transcription factor GCN4 (GCN4-RARα). We demonstrate that in vitro both proteins have transforming potential, and recapitulate the main PML-RARα biological properties, but CC-RARα is uniquely able to disrupt PML nuclear bodies. Indeed, in vivo only the CC-RARα chimera induces efficiently APL in a murine transplantation model. Thus, the PML CC domain represents the minimal structural determinant indispensable to transform RARα into an oncogenic protein.
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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.