The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity
Open accessAbstract
DNA double-stranded breaks present a serious challenge for eukaryotic cells. The inability to repair breaks leads to genomic instability, carcinogenesis and cell death. During the double-strand break response, mammalian chromatin undergoes reorganization demarcated by H2A.X Ser 139 phosphorylation (γ-H2A.X). However, the regulation of γ-H2A.X phosphorylation and its precise role in chromatin remodelling during the repair process remain unclear. Here we report a new regulatory mechanism mediated by WSTF (Williams–Beuren syndrome transcription factor, also known as BAZ1B)—a component of the WICH complex (WSTF–ISWI ATP-dependent chromatin-remodelling complex). We show that WSTF has intrinsic tyrosine kinase activity by means of a domain that shares no sequence homology to any known kinase fold. We show that WSTF phosphorylates Tyr 142 of H2A.X, and that WSTF activity has an important role in regulating several events that are critical for the DNA damage response. Our work demonstrates a new mechanism that regulates the DNA damage response and expands our knowledge of domains that contain intrinsic tyrosine kinase activity.
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DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation
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The DNA damage response: putting checkpoints in perspective
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Self-citationDNA double-strand breaks: signaling, repair and the cancer connection
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The DNA Damage Response: Ten Years After
Harper, J. W., & Elledge, S. J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.11.015 · Cited by 1,705
Self-citationATM Activation by DNA Double-Strand Breaks Through the Mre11-Rad50-Nbs1 Complex
Lee, J.-H., & Paull, T. T. (2005) · Science · doi:10.1126/science.1108297 · Cited by 1,424
Genomic Instability in Mice Lacking Histone H2AX
Celeste, A., Petersen, S., Romanienko, P. J., Fernandez-Capetillo, O., Chen, H. T., Sedelnikova, O. A., Reina-San-Martin, B., Coppola, V., Meffre, E., Difilippantonio, M. J., et al. (2002) · Science · doi:10.1126/science.1069398 · Cited by 1,385
A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling
Wysocka, J., Swigut, T., Xiao, H., Milne, T. A., Kwon, S. Y., Landry, J., Kauer, M., Tackett, A. J., Chait, B. T., Badenhorst, P., et al. (2006) · Nature · doi:10.1038/nature04815 · Cited by 1,185
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Cited by
The DNA-damage response in human biology and disease
Jackson, S. P., & Bartek, J. (2009) · Nature · doi:10.1038/nature08467 · Cited by 6,092
The DNA Damage Response: Making It Safe to Play with Knives
Ciccia, A., & Elledge, S. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.019 · Cited by 4,368
Self-citationThe Biology of Chromatin Remodeling Complexes
Clapier, C. R., & Cairns, B. R. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.062706.153223 · Cited by 2,380
Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications
Polo, S. E., & Jackson, S. P. (2011) · Genes & Development · doi:10.1101/gad.2021311 · Cited by 1,092
ATP-dependent chromatin remodeling: genetics, genomics and mechanisms
Hargreaves, D. C., & Crabtree, G. R. (2011) · Cell Research · doi:10.1038/cr.2011.32 · Cited by 923
Metadata
- Authors
- Xiao, A., Li, H., Shechter, D., Ahn, S. H., Fabrizio, L. A., Erdjument-Bromage, H., Ishibe-Murakami, S., Wang, B., Tempst, P., Hofmann, K., Patel, D. J., Elledge, S. J., & Allis, C. D.
- Venue
- Nature
- Published
- 2008-12-17
- Volume
- 457
- Issue
- 7225
- Pages
- 57-62
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2028222949
- Cited by
- 416
- References
- 46
- FWCI
- 12.53
- Type
- journal article
- Language
- en
- Open access
- green
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- Xiao, A., Li, H., Shechter, D., Ahn, S. H., Fabrizio, L. A., Erdjument-Bromage, H., Ishibe-Murakami, S., Wang, B., Tempst, P., Hofmann, K., Patel, D. J., Elledge, S. J., & Allis, C. D. (2009). WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity. Nature. https://doi.org/10.1038/nature07668
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