ArticleBiochemistry2009
Two distinct motifs within the p53 transactivation domain bind to the Taz2 domain of p300 and are differentially affected by phosphorylation.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed, 63 citations in OpenAlex.
- TAZ2 truncation confers overactivation of p300 and cellular vulnerability to HDAC inhibition.Nature communications · 2023Article
- Deciphering the acetylation code of p53 in transcription regulation and tumor suppression.Oncogene · 2022Review
- Linker DNA and histone contributions in nucleosome binding by p53.Journal of biochemistry · 2020Article
- The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with valines and intron reservoirs.Cellular and molecular life sciences : CMLS · 2020Article
- Structural insights into TAZ2 domain-mediated CBP/p300 recruitment by transactivation domain 1 of the lymphopoietic transcription factor E2A.The Journal of biological chemistry · 2020Article
- The role of acetylation sites in the regulation of p53 activity.Molecular biology reports · 2020Article
- The Dual Interactions of p53 with MDM2 and p300: Implications for the Design of MDM2 Inhibitors.International journal of molecular sciences · 2019Article
- p53 modifications: exquisite decorations of the powerful guardian.Journal of molecular cell biology · 2019Review
- NMR characterization of solvent accessibility and transient structure in intrinsically disordered proteins.Journal of biomolecular NMR · 2019Article
- Structural Basis for the Interaction between p53 Transactivation Domain and the Mediator Subunit MED25.Molecules (Basel, Switzerland) · 2018Article
- Regulation of cellular senescence via the FOXO4-p53 axis.FEBS letters · 2018Review
- The Transactivation Domains of the p53 Protein.Cold Spring Harbor perspectives in medicine · 2017Review
- p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure-Function Continuum Concept.International journal of molecular sciences · 2016Review
- Adaptive patterns in the p53 protein sequence of the hypoxia- and cancer-tolerant blind mole rat Spalax.BMC evolutionary biology · 2016Article
- Phosphorylation Regulates the Bound Structure of an Intrinsically Disordered Protein: The p53-TAZ2 Case.PloS one · 2016Article
- A Modified Reverse One-Hybrid Screen Identifies Transcriptional Activation Domains in PHYTOCHROME-INTERACTING FACTOR 3.Frontiers in plant science · 2016Article
- The 9aaTAD Transactivation Domains: From Gal4 to p53.PloS one · 2016Article
- Characterization of the p300 Taz2-p53 TAD2 complex and comparison with the p300 Taz2-p53 TAD1 complex.Biochemistry · 2015Article
- p53 Acetylation: Regulation and Consequences.Cancers · 2014Review
- Critical role for p53-serine 15 phosphorylation in stimulating transactivation at p53-responsive promoters.Nucleic acids research · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
The tumor suppressor p53 functions as a transcriptional activator for many genes, including several key genes involved in cell cycle arrest and apoptosis. Following DNA damage-induced stress, p53 undergoes extensive posttranslational modification, resulting in increased stability and activity. Two critical cofactors for p53-mediated transactivation are the histone acetyltransferase paralogues CREB-binding protein (CBP) and p300. The N-terminal transactivation domain of p53 interacts with several domains of CBP/p300, including the Taz2 domain. Here, we report the effects of specific p53 phosphorylations on its interaction with the Taz2 domain of p300. Using a competitive fluorescence anisotropy assay, we determined that monophosphorylation of p53 at Ser(15) or Thr(18) increased the affinity of p53(1-39) for Taz2, and diphosphorylations at Ser(15) and Ser(37) or Thr(18) and Ser(20) further increased the affinity. In addition, we identified a second binding site for Taz2 within p53 residues 35-59. This second site bound Taz2 with a similar affinity as the first site, but the binding was unaffected by phosphorylation. Thus, p53 posttranslational modification modulates only one of the two binding sites for p300 Taz2. Further investigation of Taz2 binding to p53(1-39) or p53(35-59) by isothermal titration calorimetry indicated that upon complex formation, the change in heat capacity at constant pressure, DeltaC(p), was negative for both sites, suggesting the importance of hydrophobic interactions. However, the more negative value of DeltaC(p) for Taz2 binding to the first (-330 cal/(mol.K)) compared to the second site (-234 cal/(mol.K)) suggests that the importance of nonpolar and polar interactions differs between the two sites.
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.