ArticleBiochemistry2007
Multiple roles for acetylation in the interaction of p300 HAT with ATF-2.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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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Who cites it
29 citing papers in PubMed, 43 citations in OpenAlex.
- DNA methylation pattern in overweight women under an energy-restricted diet supplemented with fish oil.BioMed research international · 2014Trial
- Activating transcription factors: Orchestrators of macrophage biology in pathological settings (Review).International journal of molecular medicine · 2026Review
- New insights into coordinated regulation of AHR promoter transcription; molecular mechanisms and therapeutic targets.International journal of biological sciences · 2025Review
- 2-month ketogenic diet preferentially alters skeletal muscle and augments cognitive function in middle aged female mice.Aging cell · 2022Article
- The Ras-ERK signaling pathway regulates acetylated activating transcription factor 2 via p300 in pancreatic cancer cells.Annals of translational medicine · 2020Article
- Article
- Review
- 4-Phenylbutyric Acid Protects Against Ethanol-Induced Damage in the Developing Mouse Brain.Alcoholism, clinical and experimental research · 2019Article
- Article
- Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics.Chemical reviews · 2018Review
- ATF2, a paradigm of the multifaceted regulation of transcription factors in biology and disease.Pharmacological research · 2017Review
- Molecular Basis for Histone Acetyltransferase Regulation by Binding Partners, Associated Domains, and Autoacetylation.ACS chemical biology · 2016Review
- Acetylation at lysine 71 inactivates superoxide dismutase 1 and sensitizes cancer cells to genotoxic agents.Oncotarget · 2015Article
- Protein lysine acetylation by p300/CBP.Chemical reviews · 2015Review
- Writers and readers of histone acetylation: structure, mechanism, and inhibition.Cold Spring Harbor perspectives in biology · 2014Review
- Catalytic mechanism of histone acetyltransferase p300: from the proton transfer to acetylation reaction.The journal of physical chemistry. B · 2014Article
- Structure and mechanism of non-histone protein acetyltransferase enzymes.The FEBS journal · 2013Review
- Review
- Article
- ATF2 - at the crossroad of nuclear and cytosolic functions.Journal of cell science · 2012Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The transcriptional coactivator paralogues p300 and CBP contain acetyltransferase domains (HAT) and catalyze the lysine acetylation of histones and other proteins as an important aspect of their functions. Prior studies revealed that the basic leucine zipper domain (b-ZIP) of transcription factor ATF-2 (also called CRE-BP1) can interact with the CBP HAT domain. In this study, we have examined the ATF-2 b-ZIP interaction with the p300 HAT domain and shown that p300 HAT autoacetylation can enhance the binding affinity. Pull-down assays revealed that hyperacetylated p300 HAT is more efficiently retained by immobilized ATF-2 b-ZIP than hypoacetylated p300 HAT. Loop deleted p300 HAT lacking autoacetylation was retained about as well as hyperacetylated p300 HAT, suggesting that the loop and ATF-2 compete for p300 HAT binding. While ATF-2 b-ZIP is a weak inhibitor of hypoacetylated p300 HAT acetylation of a histone H4 peptide, hyperacetylated p300 HAT is much more potently inhibited by ATF-2 b-ZIP. Moreover, we showed that ATF-2 b-ZIP could serve as an acetyltransferase substrate for p300 HAT. Using mass spectrometry, two p300 HAT lysine acetylation sites were mapped in ATF-2 b-ZIP. Immunoprecipitation-Western blot analysis with anti-acetyl-lysine antibody revealed that ATF-2 can undergo reversible acetylation in vivo. Mutational analysis of the two ATF-2 b-ZIP acetylation sites revealed their potential contributions to ATF-2-mediated transcriptional activation. Taken together, these studies suggest multiple roles for protein acetylation in the regulation of transcription by p300/CBP and ATF-2.
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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.