ArticleOncogene2012
Functional interplay between p53 acetylation and H1.2 phosphorylation in p53-regulated transcription.
Article in Oncogene, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
30 citing papers in PubMed.
- Histone Phosphorylation in DNA Damage Response.International journal of molecular sciences · 2025Review
- Comparative time-series multi-omics analyses suggest H1.2 involvement in anoxic adaptation and cancer resistance.PLoS biology · 2024Article
- An antioxidant feedforward cycle coordinated by linker histone variant H1.2 and NRF2 that drives nonsmall cell lung cancer progression.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Post-Translation Modifications and Mutations of Human Linker Histone Subtypes: Their Manifestation in Disease.International journal of molecular sciences · 2023Review
- The Highest Density of Phosphorylated Histone H1 Appeared in Prophase and Prometaphase in Parallel with Reduced H3K9me3, and HDAC1 Depletion Increased H1.2/H1.3 and H1.4 Serine 38 Phosphorylation.Life (Basel, Switzerland) · 2022Article
- H1.0 C Terminal Domain Is Integral for Altering Transcription Factor Binding within Nucleosomes.Biochemistry · 2022Article
- The roles of inducible chromatin and transcriptional memory in cellular defense system responses to redox-active pollutants.Free radical biology & medicine · 2021Review
- Binding Dynamics of Disordered Linker Histone H1 with a Nucleosomal Particle.Journal of molecular biology · 2021Article
- Molecular and Cellular Functions of the Linker Histone H1.2.Frontiers in cell and developmental biology · 2021Review
- The missing linkGenes & development · 2021Review
- Histone H1 Post-Translational Modifications: Update and Future Perspectives.International journal of molecular sciences · 2020Review
- Systematic analysis of linker histone PTM hotspots reveals phosphorylation sites that modulate homologous recombination and DSB repair.DNA repair · 2020Article
- MTA1 Promotes Hepatocellular Carcinoma Progression by Downregulation of DNA-PK-Mediated H1.2Frontiers in oncology · 2020Article
- Destabilization of linker histone H1.2 is essential for ATM activation and DNA damage repair.Cell research · 2018Article
- Dependence of Chromatosome Structure on Linker Histone Sequence and Posttranslational Modification.Biophysical journal · 2018Article
- Emerging roles of linker histones in regulating chromatin structure and function.Nature reviews. Molecular cell biology · 2018Review
- Upregulation of the ALDOA/DNA-PK/p53 pathway by dietary restriction suppresses tumor growth.Oncogene · 2018Article
- Histone H1 depletion triggers an interferon response in cancer cells via activation of heterochromatic repeats.Nucleic acids research · 2017Article
- Signaling coupled epigenomic regulation of gene expression.Oncogene · 2017Review
- Linker Histone H1.2 Directs Genome-wide Chromatin Association of the Retinoblastoma Tumor Suppressor Protein and Facilitates Its Function.Cell reports · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Linker histone H1.2 has been shown to suppress p53-dependent transcription through the modulation of chromatin remodeling; however, little is known about the mechanisms governing the antagonistic effects of H1.2 in DNA damage response. Here, we show that the repressive action of H1.2 on p53 function is negatively regulated via acetylation of p53 C-terminal regulatory domain and phosphorylation of H1.2 C-terminal tail. p53 acetylation by p300 impairs the interaction of p53 with H1.2 and triggers a rapid activation of p53-dependent transcription. Similarly, DNA-PK-mediated phosphorylation of H1.2 at T146 enhances p53 transcriptional activity by impeding H1.2 binding to p53 and thereby attenuating its suppressive effects on p53 transactivation. Consistent with these findings, point mutations mimicking modification states of H1.2 and p53 lead to a significant increase in p53-induced apoptosis. These data suggest that p53 acetylation-H1.2 phosphorylation cascade serves as a unique mechanism for triggering p53-dependent DNA damage response pathways.
Indexed as
Identifiers
What 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.