ArticleCell death and differentiation2014
Remodelling of a polypyrimidine tract-binding protein complex during apoptosis activates cellular IRESs.
Article in Cell death and differentiation, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 30 citations in OpenAlex.
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- MDM1 overexpression promotes p53 expression and cell apoptosis to enhance therapeutic sensitivity to chemoradiotherapy in patients with colorectal cancer.Cancer biology & medicine · 2025Article
- Network Analysis Performed on Transcriptomes of Parkinson's Disease Patients Reveals Dysfunction in Protein Translation.International journal of molecular sciences · 2024Article
- Established and Evolving Roles of the Multifunctional Non-POU Domain-Containing Octamer-Binding Protein (NonO) and Splicing Factor Proline- and Glutamine-Rich (SFPQ).Journal of developmental biology · 2024Review
- Integrative solution structure of PTBP1-IRES complex reveals strong compaction and ordering with residual conformational flexibility.Nature communications · 2023Article
- Polypyrimidine-Tract-Binding Protein Isoforms Differentially Regulate the Hepatitis C Virus Internal Ribosome Entry Site.Viruses · 2022Article
- PTBPs: An immunomodulatory-related prognostic biomarker in pan-cancer.Frontiers in molecular biosciences · 2022Article
- NONO and tumorigenesis: More than splicing.Journal of cellular and molecular medicine · 2020Review
- Apoptosis and Autophagy in Picornavirus Infection.Frontiers in microbiology · 2019Review
- Identification of the RNA polymerase I-RNA interactome.Nucleic acids research · 2018Article
- Alternative mechanisms of translation initiation: An emerging dynamic regulator of the proteome in health and disease.Life sciences · 2018Review
- Exploitation of nuclear functions by human rhinovirus, a cytoplasmic RNA virus.PLoS pathogens · 2018Article
- The TRPV4 channel links calcium influx to DDX3X activity and viral infectivity.Nature communications · 2018Article
- Trans-acting translational regulatory RNA binding proteins.Wiley interdisciplinary reviews. RNA · 2018Review
- An improved analysis methodology for translational profiling by microarray.RNA (New York, N.Y.) · 2017Article
- Post-transcriptional control of gene expression following stress: the role of RNA-binding proteins.Biochemical Society transactions · 2017Review
- PTBP1 modulation of MCL1 expression regulates cellular apoptosis induced by antitubulin chemotherapeutics.Cell death and differentiation · 2016Article
- Quantitative proteomics study of the neuroprotective effects of B12 on hydrogen peroxide-induced apoptosis in SH-SY5Y cells.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Post-transcriptional control of gene expression is mediated by the interaction of RNA-binding proteins with their cognate mRNAs that specifically regulate their stability, localization and translation. mRNA-binding proteins are multifunctional and it has been proposed therefore that a combinatorial RNA-binding protein code exists that allows specific protein sub-complexes to control cytoplasmic gene expression under a range of pathophysiological conditions. We show that polypyrimidine tract-binding protein (PTB) is central to one such complex that forms in apoptotic cells. Thus, during apoptosis initiated by TNF-related apoptosis inducing ligand there is a change in the repertoire of RNA-binding proteins with which PTB interacts. We show that altering the cellular levels of PTB and its binding partners, either singly or in combination, is sufficient to directly change the rates of apoptosis with increased expression of PTB, YBX1, PSF and NONO/p54(nrb) accelerating this process. Mechanistically, we show that these proteins post-transcriptionally regulate gene expression, and therefore apoptotic rates, by interacting with and stimulating the activity of RNA elements (internal ribosome entry segments) found in mRNAs that are translated during apoptosis. Taken together, our data show that PTB function is controlled by a set of co-recruited proteins and importantly provide further evidence that it is possible to dictate cell fate by modulating cytoplasmic gene expression pathways alone.
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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.