Cited by 113DNA Repair MechanismsGenomics and Chromatin DynamicsCancer-related Molecular Pathways

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Identification and characterization of FUS/TLS as a new target of ATM

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Gardiner, Mary, Toth, Rachel, Vandermoere, Franck, Morrice, Nicholas A., Rouse, John·2008·Biochemical Journal

DOI 10.1042/bj20081135

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Abstract

ATM (ataxia-telangiectasia mutated), ATR (ATM- and Rad3-related) and DNA-PK (DNA-dependent protein kinase), important regulators of genome stability, belong to the PIKK (phosphoinositide 3-kinase-like kinase) family of protein kinases. In the present study, DNA-affinity chromatography was used to identify DNA-binding proteins phosphorylated by these kinases. This resulted in the identification of FUS (fused in sarcoma)/TLS (translocated in liposarcoma) as an in vitro target of the PIKKs. FUS is a member of the Ewing's sarcoma family of proteins that appears to play a role in regulating genome stability, since mice lacking FUS show chromosomal instability and defects in meiosis. The residues in FUS that are phosphorylated in vitro and in vivo were identified, and phospho-specific antibodies were generated to demonstrate that FUS becomes phosphorylated at Ser42in vivo, primarily in response to agents that cause DSBs (double-strand breaks). DSB-induced FUS phosphorylation in vivo at Ser42 requires ATM and not DNA-PK. Although Ser42 is retained in the oncogenic FUS–CHOP [C/EBP (CCAAT/enhancer-binding protein)-homologous protein 10] fusion generated by a t(12;16)(q13;p11) chromosomal translocation, Ser42 in FUS–CHOP is not phosphorylated after DNA damage. These results identify FUS as a new target of the ATM-signalling pathway and strengthen the notion that FUS regulates genome stability.

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ATM and ATR Substrate Analysis Reveals Extensive Protein Networks Responsive to DNA Damage
Matsuoka, S., Ballif, B. A., Smogorzewska, A., McDonald, E. R., Hurov, K. E., Luo, J., Bakalarski, C. E., Zhao, Z., Solimini, N., Lerenthal, Y., et al. (2007) · Science · doi:10.1126/science.1140321 · Cited by 3,075
ATM and related protein kinases: safeguarding genome integrity
Shiloh, Y. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1011 · Cited by 2,577
Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damage
Falck, J., Coates, J., & Jackson, S. P. (2005) · Nature · doi:10.1038/nature03442 · Cited by 1,301
Identification and characterization of a novel and specific inhibitor of the ataxia-telangiectasia mutated kinase ATM
Hickson, I., Zhao, Y., Richardson, C. J., Green, S. J., Martin, N. M. B., Orr, A. I., Reaper, P. M., Jackson, S. P., Curtin, N. J., & Smith, G. C. M. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-2727 · Cited by 1,220
The RNA recognition motif, a plastic RNA‐binding platform to regulate post‐transcriptional gene expression
Maris, C., Dominguez, C., & Allain, F. H. ‐. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04653.x · Cited by 1,135
DNA excision repair
Sancar, A. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.000355 · Cited by 1,131
The Bloom's syndrome helicase suppresses crossing over during homologous recombination
Wu, L., & Hickson, I. D. (2003) · Nature · doi:10.1038/nature02253 · Cited by 1,087
The DNA-dependent protein kinasePreprint
Smith, G. C. M., & Jackson, S. P. (1999) · Genes & Development · doi:10.1101/gad.13.8.916 · Cited by 903
Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma
Crozat, A., Åman, P., Mandahl, N., & Ron, D. (1993) · Nature · doi:10.1038/363640a0 · Cited by 897
Catalysis of ATP-Dependent Homologous DNA Pairing and Strand Exchange by Yeast RAD51 Protein
Sung, P. (1994) · Science · doi:10.1126/science.8066464 · Cited by 869

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Authors: Gardiner, M., Toth, R., Vandermoere, F., Morrice, N. A., & Rouse, J.
Affiliations: University of Dundee (GB)
ORCID: Toth, Rachel
Vandermoere, Franck
Rouse, John
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2008-09-25
Volume: 415
Issue: 2
Pages: 297-307
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20081135
OpenAlex: W2023532020
Cited by: 111
References: 53
Citations by year: 2026: 1 · 2025: 3 · 2024: 3 · 2023: 8 · 2022: 6 · 2021: 12 · 2020: 7 · 2019: 8 · 2018: 9 · 2017: 6 · 2016: 11 · 2015: 4 · 2014: 6 · 2013: 4 · 2012: 5
FWCI: 2.47
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (publishedVersion)
HAL (submittedVersion, other-oa)
Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion, other-oa)
Funders: Medical Research Council
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
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Keywords: FUS, TLS, ATM, PIKK kinases, protein phosphorylation, DNA double-strand breaks, DNA damage response, genome stability, chromosomal instability, DNA-binding proteins
MeSH terms: Amino Acid Sequence, Cell Line, Chromatography, Affinity, DNA Damage, DNA-Binding Proteins, Humans, Molecular Sequence Data, Phosphorylation, Recombinant Fusion Proteins, Serine, Mass Spectrometry, Ultraviolet Rays, Protein Serine-Threonine Kinases, Sequence Homology, Amino Acid, Cell Cycle Proteins, Tumor Suppressor Proteins, RNA-Binding Protein FUS, DNA-Activated Protein Kinase, Ataxia Telangiectasia Mutated Proteins

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Identification and characterization of FUS/TLS as a new target of ATM

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