ArticleOncogene2000
The promyelocytic leukemia (PML) protein suppresses cyclin D1 protein production by altering the nuclear cytoplasmic distribution of cyclin D1 mRNA.
Article in Oncogene, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 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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Who cites it
42 citing papers in PubMed, 93 citations in OpenAlex.
- Med9 Is a Novel eIF4E-Interacting Protein inInternational journal of molecular sciences · 2026Article
- PML Nuclear bodies: the cancer connection and beyond.Nucleus (Austin, Tex.) · 2024Review
- eIF4E orchestrates mRNA processing, RNA export and translation to modify specific protein production.Nucleus (Austin, Tex.) · 2024Review
- Biological functions and research progress of eIF4E.Frontiers in oncology · 2023Review
- Localization and Functional Roles of Components of the Translation Apparatus in the Eukaryotic Cell Nucleus.Cells · 2021Review
- PML: Regulation and multifaceted function beyond tumor suppression.Cell & bioscience · 2018Review
- Identification of a novel RNA giant nuclear body in cancer cells.Oncotarget · 2016Article
- The RNA-Binding Protein, Polypyrimidine Tract-Binding Protein 1 (PTBP1) Is a Key Regulator of CD4 T Cell Activation.PloS one · 2016Article
- Deletion of Methionine Sulfoxide Reductase A Does Not Affect Atherothrombosis but Promotes Neointimal Hyperplasia and Extracellular Signal-Regulated Kinase 1/2 Signaling.Arteriosclerosis, thrombosis, and vascular biology · 2015Article
- The Eukaryotic Translation Initiation Factor 4E (eIF4E) as a Therapeutic Target for Cancer.Advances in protein chemistry and structural biology · 2015Review
- The eukaryotic translation initiation factor eIF4E in the nucleus: taking the road less traveled.Immunological reviews · 2015Review
- An eIF4E-interacting peptide induces cell death in cancer cell lines.Cell death & disease · 2014Article
- Is PML a Tumor Suppressor?Frontiers in oncology · 2013Article
- The p53 target gene TRIM22 directly or indirectly interacts with the translation initiation factor eIF4E and inhibits the binding of eIF4E to eIF4G.Biology of the cell · 2012Article
- RNA-related nuclear functions of human Pat1b, the P-body mRNA decay factor.Molecular biology of the cell · 2012Article
- Review
- Interwoven roles of cyclin D3 and cdk4 recruited by ICP0 and ICP4 in the expression of herpes simplex virus genes.Journal of virology · 2010Article
- PML nuclear bodies.Cold Spring Harbor perspectives in biology · 2010Review
- A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics.International journal of biological sciences · 2010Review
- Understanding and Targeting the Eukaryotic Translation Initiation Factor eIF4E in Head and Neck Cancer.Journal of oncology · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The majority of the promyelocytic leukemia (PML) protein is present in nuclear bodies which are altered in several pathogenic conditions including acute promyelocytic leukemia. PML nuclear bodies are found in nearly all cells yet their function remains unknown. Here, we demonstrate that PML and the eukaryotic initiation factor 4E (elF-4E) co-localize and co-immunopurify. eIF-4E is involved in nucleocytoplasmic transport of specific mRNAs including cyclin D1. eIF-4E overexpression leads to increased cyclin D1 protein levels; whereas, overexpression of PML leads to decreased cyclin D1 levels. Neither PML nor eIF-4E cause significant changes in cyclin D1 mRNA levels. The association with eIF-4E led us to investigate if PML could alter mRNA distribution as a possible post-transcriptional mechanism for suppressing cyclin D1 production. We show that overexpression of PML results in nuclear retention of cyclin D1 mRNA and that intact PML nuclear bodies are required. Addition of eIF-4E overcomes PML induced retention and alters the morphology of PML bodies suggesting a mechanism by which eIF-4E can modulate PML function. These results raise the possibility that PML nuclear bodies may participate in the regulation of nucleocytoplasmic transport of specific mRNAs.
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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.