ArticleProceedings of the National Academy of Sciences of the United States of America2003
Y box-binding protein 1 induces resistance to oncogenic transformation by the phosphatidylinositol 3-kinase pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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.
The trial behind it
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
36 citing papers in PubMed, 68 citations in OpenAlex.
- Y-Box Binding Protein 1: Unraveling the Multifaceted Role in Cancer Development and Therapeutic Potential.International journal of molecular sciences · 2024Review
- YB-1 Is a Novel Target for the Inhibition of α-Adrenergic-Induced Hypertrophy.International journal of molecular sciences · 2023Article
- A TLR/CD44 axis regulates T cell trafficking in experimental and human multiple sclerosis.iScience · 2022Article
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- Blocking Y-Box Binding Protein-1 through Simultaneous Targeting of PI3K and MAPK in Triple Negative Breast Cancers.Cancers · 2020Article
- YB-1 Knockdown Inhibits the Proliferation of Mesothelioma Cells through Multiple Mechanisms.Cancers · 2020Article
- Crosstalk between Akt signaling and cold shock proteins in mediating invasive cell phenotypes.Oncotarget · 2018Article
- The tumor-associated YB-1 protein: new player in the circadian control of cell proliferation.Oncotarget · 2017Article
- Role of Y Box Protein-1 in cancer: As potential biomarker and novel therapeutic target.Journal of Cancer · 2017Review
- Etoposide enhances antitumor efficacy of MDR1-driven oncolytic adenovirus through autoupregulation of the MDR1 promoter activity.Oncotarget · 2015Article
- Akt-mediated phosphorylation controls the activity of the Y-box protein MSY3 in skeletal muscle.Skeletal muscle · 2015Article
- JNK1/2 Activation by an Extract from the Roots of Morus alba L. Reduces the Viability of Multidrug-Resistant MCF-7/Dox Cells by Inhibiting YB-1-Dependent MDR1 Expression.Evidence-based complementary and alternative medicine : eCAM · 2013Article
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- YB-1 binds to GluR2 mRNA and CaM1 mRNA in the brain and regulates their translational levels in an activity-dependent manner.Cellular and molecular neurobiology · 2010Article
- Phosphatidylinositol 3-kinase: the oncoprotein.Current topics in microbiology and immunology · 2010Review
- Akt-mediated regulation of NFkappaB and the essentialness of NFkappaB for the oncogenicity of PI3K and Akt.International journal of cancer · 2009Article
- General RNA-binding proteins have a function in poly(A)-binding protein-dependent translation.The EMBO journal · 2009Article
- Constitutively active Rheb induces oncogenic transformation.Oncogene · 2008Article
- YB-1 promotes microtubule assembly in vitro through interaction with tubulin and microtubules.BMC biochemistry · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Y box-binding protein 1 (YB-1) is a multifunctional protein that can act as a regulator of transcription and of translation. In chicken embryo fibroblasts transformed by the oncoproteins P3k (phosphatidylinositol 3-kinase) or Akt, YB-1 is transcriptionally down-regulated. Expression of YB-1 from a retroviral vector induces a strong cellular resistance to transformation by P3k or Akt but does not affect sensitivity to transformation by other oncoproteins, such as Src, Jun, or Qin. The YB-1-expressing cells assume a tightly adherent, flat phenotype, with YB-1 localized in the cytoplasm, and show a greatly reduced saturation density. Both cap-dependent and cap-independent translation is inhibited in these cells, but the activity of Akt remains unaffected, suggesting that YB-1 functions downstream of Akt. A YB-1 protein with a loss-of-function mutation in the RNA-binding motif no longer binds to the mRNA cap structure, is localized in the cell nucleus, does not induce the flat cellular phenotype, and fails to interfere with P3k- or Akt-induced oncogenic transformation. This mutant also does not inhibit cap-dependent or cap-independent translation. These results suggest that YB-1 acts like a rapamycin mimic, inhibiting translational events that are required in phosphatidylinositol 3-kinase-driven oncogenic transformation.
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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.