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KAT5 tyrosine phosphorylation couples chromatin sensing to ATM signalling
Open accessAbstract
The detection of DNA lesions within chromatin represents a critical step in cellular responses to DNA damage. However, the regulatory mechanisms that couple chromatin sensing to DNA-damage signalling in mammalian cells are not well understood. Here we show that tyrosine phosphorylation of the protein acetyltransferase KAT5 (also known as TIP60) increases after DNA damage in a manner that promotes KAT5 binding to the histone mark H3K9me3. This triggers KAT5-mediated acetylation of the ATM kinase, promoting DNA-damage-checkpoint activation and cell survival. We also establish that chromatin alterations can themselves enhance KAT5 tyrosine phosphorylation and ATM-dependent signalling, and identify the proto-oncogene c-Abl as a mediator of this modification. These findings define KAT5 tyrosine phosphorylation as a key event in the sensing of genomic and chromatin perturbations, and highlight a key role for c-Abl in such processes.
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“H3K9me3 is required for activation of the Tip60 acetyltransferase (4, 17).”
From DNA double-strand breaks promote methylation of histone H3 on lysine 9 and transient formation of repressive chromatin (2014) · cites this paper as [17]
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In the citing paper
“Consequently, loss of H3K9me2/3 leads to failure to activate the ATM signaling pathway, loss of H4 acetylation during DSB repair, disruption of heterochromatin, genomic instability, and defective DSB repair (4,(17)(18)(19).”
From DNA double-strand breaks promote methylation of histone H3 on lysine 9 and transient formation of repressive chromatin (2014) · cites this paper as [17]
Experimental — accuracy not yet measuredIn the citing paper
“phosphorylation enhances the acetyltransferase activity of TIP60, and this modification can be induced by chromatin alterations, leading to ATM signaling independently of DNA breaks”
From Activation of DNA Damage Response Signaling by Condensed Chromatin (2014) · cites this paper as Kaidi and Jackson, 2013
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Metadata
- Authors
- Kaidi, A., & Jackson, S. P.
- Affiliations
- University of Cambridge (GB)
- Corresponding author
- Jackson, Stephen P.
- Venue
- Nature
- Published
- 2013-05-26
- Volume
- 498
- Issue
- 7452
- Pages
- 70-74
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3859897
- OpenAlex
- W2045041347
- Cited by
- 167
- References
- 35
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 3 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 2 · 2019: 15 · 2018: 27 · 2017: 21 · 2016: 26 · 2015: 32 · 2014: 20 · 2013: 12
- FWCI
- 13.43
- Type
- journal article
- Language
- en
- Status
- Retracted
- Update notices
- retraction (2019-04-11)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Bristol Research (University of Bristol) (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Wellcome Trust (WT092096, 092096)
- Cancer Research UK (C6/A11224, 11224, A11224)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- KAT5, Tip60, tyrosine phosphorylation, c-Abl, ATM kinase, H3K9me3, histone acetylation, DNA damage checkpoint, DNA double-strand breaks, histone acetyltransferase
- MeSH terms
- Lysine Acetyltransferase 5, Proto-Oncogene Mas, Amino Acid Sequence, Animals, Cell Line, Cell Survival, Chromatin, DNA Damage, DNA-Binding Proteins, Enzyme Activation, HeLa Cells, Histones, Humans, Lysine, Methylation, Molecular Sequence Data, Phosphorylation, Signal Transduction, Proto-Oncogene Proteins c-abl, Protein Serine-Threonine Kinases, Cell Cycle Proteins, Phosphotyrosine, Tumor Suppressor Proteins, Histone Acetyltransferases, Cell Cycle Checkpoints, Ataxia Telangiectasia Mutated Proteins
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