The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
Requirement of ATM-Dependent Monoubiquitylation of Histone H2B for Timely Repair of DNA Double-Strand Breaks
Open accessAbstract
SUMMARY The cellular response to DNA double-strand breaks (DSBs) is mobilized by the protein kinase ATM, which phosphorylates key players in the DNA damage response (DDR) network. A major question is how ATM controls DSB repair. Optimal repair requires chromatin relaxation at damaged sites. Chromatin reorganization is coupled to dynamic alterations in histone posttranslational modifications. Here, we show that in human cells, DSBs induce monoubiquitylation of histone H2B, a modification that is associated in undamaged cells with transcription elongation. We find that this process relies on recruitment to DSB sites and ATM-dependent phosphorylation of the responsible E3 ubiquitin ligase: the RNF20-RNF40 heterodimer. H2B monoubiquitylation is required for timely recruitment of players in the two major DSB repair pathways—nonhomologous end-joining and homologous recombination repair—and optimal repair via both pathways. Our data and previous data suggest a two-stage model for chromatin decondensation that facilitates DSB repair.
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Cites
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DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation
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ATM and ATR Substrate Analysis Reveals Extensive Protein Networks Responsive to DNA Damage
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Self-citationThe mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway
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XRCC3 promotes homology-directed repair of DNA damage in mammalian cells
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Cited by
The ATM protein kinase: regulating the cellular response to genotoxic stress, and more
Shiloh, Y., & Ziv, Y. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3546 · Cited by 1,649
Self-citationDNA double-strand break repair-pathway choice in somatic mammalian cells
Scully, R., Panday, A., Elango, R., & Willis, N. A. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0152-0 · Cited by 1,457
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Regulation of nucleosome dynamics by histone modifications
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Breaking the chains: deubiquitylating enzyme specificity begets function
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Metadata
- Authors
- Moyal, L., Lerenthal, Y., Gana-Weisz, M., Mass, G., So, S., Wang, S.-Y., Eppink, B., Chung, Y. M., Shalev, G., Shema, E., Shkedy, D., Smorodinsky, N. I., van Vliet, N., Kuster, B., Mann, M., Ciechanover, A., Dahm-Daphi, J., Kanaar, R., Hu, M. C.-T., Chen, D. J., Oren, M., & Shiloh, Y.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2011-03
- Volume
- 41
- Issue
- 5
- Pages
- 529-542
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2152385412
- Cited by
- 403
- References
- 58
- FWCI
- 13.64
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Moyal, L., Lerenthal, Y., Gana-Weisz, M., Mass, G., So, S., Wang, S.-Y., Eppink, B., Chung, Y. M., Shalev, G., Shema, E., Shkedy, D., Smorodinsky, N. I., van Vliet, N., Kuster, B., Mann, M., Ciechanover, A., Dahm-Daphi, J., Kanaar, R., Hu, M. C.-T., . . . Shiloh, Y. (2011). Requirement of ATM-Dependent Monoubiquitylation of Histone H2B for Timely Repair of DNA Double-Strand Breaks. Molecular Cell. https://doi.org/10.1016/j.molcel.2011.02.015
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