ArticleMolecular and cellular biology2009
Regulation of protein synthesis by ionizing radiation.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed, 132 citations in OpenAlex.
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- Collagen XVII inhibits breast cancer cell proliferation and growth through deactivation of the AKT/mTOR signaling pathway.PloS one · 2021Article
- Proteomics Reveals Distinct Changes Associated with Increased Gamma Radiation Resistance in the Black YeastGenes · 2020Article
- Ionizing Radiation and Translation Control: A Link to Radiation Hormesis?International journal of molecular sciences · 2020Review
- Autophagy in fate determination of mesenchymal stem cells and bone remodeling.World journal of stem cells · 2020Review
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- The Transcriptomic and Phenotypic Response of the Melanized YeastFrontiers in microbiology · 2020Article
- DNA damage responses in murine Pre-B cells with genetic deficiencies in damage response genes.Cell cycle (Georgetown, Tex.) · 2020Article
- An Effective Protocol for Proteome Analysis of Medaka (Methods and protocols · 2019Article
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- Doxorubicin-induced DNA Damage Causes Extensive Ubiquitination of Ribosomal Proteins Associated with a Decrease in Protein Translation.Molecular & cellular proteomics : MCP · 2018Article
- Radiosensitizing effects of Sestrin2 in PC3 prostate cancer cells.Iranian journal of basic medical sciences · 2018Article
- ER stress and genomic instability induced by gamma radiation in mice primary cultured glial cells.Metabolic brain disease · 2018Article
18 more citing papers are in PubMed but not listed here.
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 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ionizing radiation (IR) is a physiologically important stress to which cells respond by the activation of multiple signaling pathways. Using a panel of immortalized and transformed breast epithelial cell lines, we demonstrate that IR regulation of protein synthesis occurs in nontransformed cells and is lost with transformation. In nontransformed cells, IR rapidly activates the MAP kinases ERK1/2, resulting in an early transient increase in cap-dependent mRNA translation that involves mTOR and is radioprotective, enhancing the translation of a subset of mRNAs encoding proteins involved in DNA repair and cell survival. Following a transient increase in translation, IR-sensitive (nontransformed) cells inhibit cap-dependent protein synthesis through a mechanism that involves activation of p53, induction of Sestrin 1 and 2 genes, and stimulation of AMP kinase, inhibiting mTOR and hypophosphorylating 4E-BP1. IR is shown to block proteasome-mediated decay of 4E-BP1, increasing its abundance and the sequestration of eIF4E. The IR signal that impairs mTOR-dependent protein synthesis at late times is assembly of the DNA damage response machinery, consisting of Mre11, Rad50, and NBS1 (MRN); activation of the MRN complex kinase ATM; and p53. These results link genotoxic signaling from the DNA damage response complex to the control of protein synthesis.
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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.