KAT5 tyrosine phosphorylation couples chromatin sensing to ATM signalling

Kaidi, Abderrahmane; Jackson, Stephen P.

doi:10.1038/nature12201

Cited by 167DNA Repair MechanismsGenomics and Chromatin DynamicsChromatin Remodeling and Cancer

KAT5 tyrosine phosphorylation couples chromatin sensing to ATM signalling

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Kaidi, Abderrahmane, Jackson, Stephen P.·2013·Nature

DOI 10.1038/nature12201PMC PMC3859897

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Abstract

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.
“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]
The ‘Tyrosine phosphorylation-mediated enhancement of KAT5 activity’ section reports that H3K9me3 peptide stimulates KAT5-mediated ATM acetylation under specific conditions. It also says the peptide does not affect KAT5 activity toward histone H4, so the paper does not establish that H3K9me3 is required for activation of the acetyltransferase generally. No page number is available in our copy. (LLM, conf=0.87)
Experimental — accuracy not yet measured
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.
“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]
The Abstract and the section on KAT5 activity link H3K9me3 binding to KAT5-mediated ATM acetylation and enhanced ATM signaling. They do not establish that loss of H3K9me2/3 causes complete failure of ATM activation, heterochromatin disruption, genomic instability, or defective DSB repair. The KAT5 activity section instead reports that H3K9me3 peptide binding did not affect KAT5 activity toward histone H4, so it does not support the claimed loss of H4 acetylation. (LLM, conf=0.87)
Experimental — accuracy not yet measured
Phosphorylation enhances TIP60 acetyltransferase activity and can be induced by chromatin alterations, leading to ATM signaling independently of DNA breaks.
“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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Authors: Kaidi, A., & Jackson, S. P.
Affiliations: University of Cambridge (GB)
Corresponding author: Jackson, Stephen P.
ORCID: Kaidi, Abderrahmane
Jackson, Stephen P.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2013-05-26
Volume: 498
Issue: 7452
Pages: 70-74
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature12201
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
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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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KAT5 tyrosine phosphorylation couples chromatin sensing to ATM signalling

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