ArticleNature structural & molecular biology2012
PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53.
Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 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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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.
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Who cites it
57 citing papers in PubMed, 97 citations in OpenAlex.
- A revised model for PHF20L1 Tudor function: DNA binding overrides methylation selectivity on nucleosomes.The Journal of biological chemistry · 2026Article
- Identification of microprotein-coding intronic polyadenylation isoforms and function in genotoxic anticancer drug response.Genome biology · 2025Article
- Homozygous Deletion of the Epigenetic RegulatorHuman mutation · 2025Article
- Exploring the various functions of PHD finger protein 20: beyond the unknown.Toxicological research · 2025Review
- Enhancement of renal fibrosis in PHF20 transgenic mice.Toxicological research · 2025Article
- Lysine and arginine methylation of transcription factors.Cellular and molecular life sciences : CMLS · 2024Review
- Molecular dynamics-based computational investigations on the influence of tumor suppressor p53 binding protein against other proteins/peptides.Scientific reports · 2024Article
- Genetic Association and Differential RNA Expression of Histone (De)Acetylation-Related Genes in Pemphigus Foliaceus-A Possible Epigenetic Effect in the Autoimmune Response.Life (Basel, Switzerland) · 2023Article
- Mettl13 protects against cardiac contractile dysfunction by negatively regulating C-Cbl-mediated ubiquitination of SERCA2a in ischemic heart failure.Science China. Life sciences · 2023Article
- An autoinhibited state of 53BP1 revealed by small molecule antagonists and protein engineering.Nature communications · 2023Article
- GART Functions as a Novel Methyltransferase in the RUVBL1/β-Catenin Signaling Pathway to Promote Tumor Stemness in Colorectal Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Methylation across the central dogma in health and diseases: new therapeutic strategies.Signal transduction and targeted therapy · 2023Review
- Genome- and transcriptome-wide association studies of 386,000 Asian and European-ancestry women provide new insights into breast cancer genetics.American journal of human genetics · 2022Article
- PHF20 is crucial for epigenetic control of starvation-induced autophagy through enhancer activation.Nucleic acids research · 2022Article
- Deciphering the PTM codes of the tumor suppressor p53.Journal of molecular cell biology · 2022Review
- Construction of a prognostic model related to copper dependence in breast cancer by single-cell sequencing analysis.Frontiers in genetics · 2022Article
- Assessing kinetics and recruitment of DNA repair factors using high content screens.Cell reports · 2021Article
- Identification of early and intermediate biomarkers for ARDS mortality by multi-omic approaches.Scientific reports · 2021Observational
- Searching for Biological Function of the Mysterious PA2504 Protein fromInternational journal of molecular sciences · 2021Article
- Methyl-Induced Polarization Destabilizes the Noncovalent Interactions of N-Methylated Lysines.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 2 countries.
Funding
Abstract
PHF20 is a multidomain protein and subunit of a lysine acetyltransferase complex that acetylates histone H4 and p53 but whose function is unclear. Using biochemical, biophysical and cellular approaches, we determined that PHF20 is a direct regulator of p53. A Tudor domain in PHF20 recognized p53 dimethylated at Lys370 or Lys382 and a homodimeric form of this Tudor domain could associate with the two dimethylated sites on p53 with enhanced affinity, indicating a multivalent interaction. Association with PHF20 promotes stabilization and activation of p53 by diminishing Mdm2-mediated p53 ubiquitylation and degradation. PHF20 contributes to upregulation of p53 in response to DNA damage, and ectopic expression of PHF20 in different cell lines leads to phenotypic changes that are hallmarks of p53 activation. Overall our work establishes that PHF20 functions as an effector of p53 methylation that stabilizes and activates p53.
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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.