ArticleOncogene2008
Phosphorylation by Akt disables the anti-oncogenic activity of YB-1.
Article in Oncogene, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed.
- Comprehensive pan-cancer analysis of YBX family reveals YBX2 as a potential biomarker in liver cancer.Frontiers in immunology · 2024Article
- YB-1 activating cascades as potential targets in KRAS-mutated tumors.Strahlentherapie und Onkologie : Organ der Deutschen Rontgengesellschaft ... [et al] · 2023Review
- YB-1 unwinds mRNA secondary structures in vitro and negatively regulates stress granule assembly in HeLa cells.Nucleic acids research · 2021Article
- Blocking Y-Box Binding Protein-1 through Simultaneous Targeting of PI3K and MAPK in Triple Negative Breast Cancers.Cancers · 2020Article
- Structural basis of DNA binding to human YB-1 cold shock domain regulated by phosphorylation.Nucleic acids research · 2020Article
- Y-Box Binding Proteins in mRNP Assembly, Translation, and Stability Control.Biomolecules · 2020Review
- Antisense Oligonucleotides Targeting Y-Box Binding Protein-1 Inhibit Tumor Angiogenesis by Downregulating Bcl-xL-VEGFR2/-Tie Axes.Molecular therapy. Nucleic acids · 2017Article
- RSK-mediated nuclear accumulation of the cold-shock Y-box protein-1 controls proliferation of T cells and T-ALL blasts.Cell death and differentiation · 2017Article
- Article
- Akt-mediated phosphorylation controls the activity of the Y-box protein MSY3 in skeletal muscle.Skeletal muscle · 2015Article
- YB-1 expression promotes epithelial-to-mesenchymal transition in prostate cancer that is inhibited by a small molecule fisetin.Oncotarget · 2014Article
- The role of cold shock domain proteins in inflammatory diseases.Journal of molecular medicine (Berlin, Germany) · 2014Review
- The feed-forward loop between YB-1 and MYC is essential for multiple myeloma cell survival.Leukemia · 2013Article
- Cancer biology: The director's cut.Nature · 2012Article
- RNA-binding proteins as a point of convergence of the PI3K and p38 MAPK pathways.Frontiers in immunology · 2012Article
- Suppression of Her2/neu expression through ILK inhibition is regulated by a pathway involving TWIST and YB-1.Oncogene · 2010Article
- Functional phosphoproteomic analysis reveals cold-shock domain protein A to be a Bcr-Abl effector-regulating proliferation and transformation in chronic myeloid leukemia.Cell death & disease · 2010Article
- Post-transcriptional up-regulation of Tsc-22 by Ybx1, a target of miR-216a, mediates TGF-{beta}-induced collagen expression in kidney cells.The Journal of biological chemistry · 2010Article
- 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
- Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Y box-binding protein 1 (YB-1) is a DNA/RNA-binding protein that regulates mRNA transcription and translation. It is a major component of free messenger ribonucleoprotein particles and, at higher concentrations, blocks protein synthesis. In chicken embryo fibroblasts, overexpression of YB-1 confers a specific resistance to oncogenic cellular transformation by phosphoinositide 3-kinase (PI3K) or Akt/PKB. Recent studies have identified YB-1 as a direct substrate of Akt. The functional significance of Akt-mediated phosphorylation remains largely unknown. We generated YB-1 mutants in the Akt phosphorylation consensus sequence to explore the effect of phosphorylated YB-1 in PI3K-induced transformation. In contrast to wild-type YB-1, the phosphomimetic S99E mutant no longer interferes with cellular transformation. This mutant has reduced affinity for the cap of mRNAs and fails to inhibit cap-dependent translation. The data suggest that phosphorylation by Akt disables the inhibitory activity of YB-1 and thereby enhances the translation of transcripts that are necessary for oncogenesis. Overexpression of wild-type YB-1 overrides inactivation by Akt and maintains inhibition of protein synthesis and resistance to transformation.
Indexed as
Identifiers
17704806What OpenQuestion holds
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.