ArticleOncotarget2017
NEURL4 regulates the transcriptional activity of tumor suppressor protein p53 by modulating its oligomerization.
Article in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 23 citations in OpenAlex.
- A simplified in vitro disease-mimicking culture system can determine the angiogenic effect of medicines on vascular diseases.Cytotechnology · 2025Article
- The disordered negatively charged C-terminus of the large HECT E3 ubiquitin ligase HERC2 provides structural and thermal stability to the HECT C-lobe.Protein science : a publication of the Protein Society · 2024Article
- Protective effect of Huanglian Pingwei San on DSS-induced ulcerative colitis in mice through amelioration of the inflammatory response and oxidative stress.Frontiers in pharmacology · 2024Article
- The ATMolecules (Basel, Switzerland) · 2023Review
- HERC2 deficiency activates C-RAF/MKK3/p38 signalling pathway altering the cellular response to oxidative stress.Cellular and molecular life sciences : CMLS · 2022Article
- Genome-wide analysis of genes encoding core components of the ubiquitin system during cerebral cortex development.Molecular brain · 2022Article
- Serum TP53 Protein Level as a Sensitive Biomarker for the Diagnosis of Myocardial Damage in Children.Medical science monitor : international medical journal of experimental and clinical research · 2022Article
- Neuralized-like protein 4 (NEURL4) mediates ADP-ribosylation of mitochondrial proteins.The Journal of cell biology · 2022Article
- The role of p53 in liver fibrosis.Frontiers in pharmacology · 2022Review
- Involvement of p53, p21, and Caspase-3 in Apoptosis of Coronary Artery Smooth Muscle Cells in a Kawasaki Vasculitis Mouse Model.Medical science monitor : international medical journal of experimental and clinical research · 2020Article
- HERC Ubiquitin Ligases in Cancer.Cancers · 2020Review
- Regulation of the MDM2-p53 pathway by the ubiquitin ligase HERC2.Molecular oncology · 2020Article
- Integrative genomic analysis identifies associations of molecular alterations to APOBEC and BRCA1/2 mutational signatures in breast cancer.Molecular genetics & genomic medicine · 2019Article
- Large HERCs Function as Tumor Suppressors.Frontiers in oncology · 2019Article
- HERCing: Structural and Functional Relevance of the Large HERC Ubiquitin Ligases.Frontiers in physiology · 2019Review
- Assembly of human C-terminal binding protein (CtBP) into tetramers.The Journal of biological chemistry · 2018Article
- NAD(H) phosphates mediate tetramer assembly of human C-terminal binding protein (CtBP).The Journal of biological chemistryArticle
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p53 is a transcription factor that regulates important cellular processes related to tumor suppression, including induction of senescence, apoptosis, and DNA repair as well as the inhibition of angiogenesis and cell migration. Therefore, it is critical to understand the molecular mechanism that regulates it. p53 tetramerization is a key step in its activation process and the regulation of this oligomerization, an important control point. The E3 ubiquitin ligase HERC2 controls the p53 transcriptional activity by regulation of its oligomerization state. HERC2-interacting proteins such as the adaptor-like protein with six neuralized domains NEURL4 are also candidates to regulate p53 activity. Here, we demonstrate the existence of an interaction network between NEURL4, HERC2 and p53 proteins. We report a functional interaction between NEURL4 and p53, involving the C-terminal region of p53 and the neuralized domains 3 and 4 of NEURL4. Through this interaction, NEURL4 regulates the transcriptional activity of p53. Thus, NEURL4 depletion reduced the transcriptional activity whereas NEURL4 overexpression increased it. In both cases, p53 stability was not affected. Although NEURL4 may interact with p53 independently of the E3 ubiquitin ligase HERC2, we observed that both proteins are needed to regulate the transcriptional activity of p53. Clonogenic assays confirmed the functional relevance of this interaction observing a decrease in cell growth by NEURL4 overexpression correlated to the increase of cellular cycle inhibitor p21 by p53 activation. Under these conditions, NEURL4 activated p53 oligomerization. All these findings identify NEURL4 as a novel regulator of the p53's signaling.
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