Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks

By Y. Huyen, O. Zgheib, Richard A. DiTullio, Vassilis G. Gorgoulis, Panayotis Zacharatos, Tom J. Petty, Emily A. Sheston, H. Mellert, E. Stavridi, T. Halazonetis. Nature, 2004

935 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/840eac738e349596285a3684c182078e3eb4bf65

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Citations in the corpus

• RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. (2007, background): “Given the role of histone ubiquitylation in chromatin remodeling, it is also plausible that the RNF8-dependent ubiquitylation events at the vicinity of DNA breaks may enhance the accessibility of 53BP1 to modified histones (Huyen et al., 2004; Sanders et al., 2004; Botuyan et al., 2006).”
• RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. (2009, positive): “Furthermore, accumulation of 53BP1 at DSBs requires also constitutive epigenetic marks (such as dimethylated K79 of histone H3 and/or dimethylated K20 of histone H4), which are recognized by the Tudor domain of 53BP1 (Botuyan et al., 2006; Huyen et al., 2004).”
• 53BP1 is a reader of the DNA damage-induced H2A Lys15 ubiquitin mark (2013, neutral): “Class switching to IgG1 was assayed in 53BP1 murine primary B cells complemented with 53BP1 (1-1711) and mutants thereof by retroviral delivery.”
• Surviving the breakup: the DNA damage checkpoint. (2006, background): “ATM (Ataxia-Telangiectasia Mutated) was identified as the gene mutated in the inherited cancer predisposition syndrome ataxia telangiectasia (A-T), and is a key player in the response to double-strand chromosomal breaks (DSBs) (1).”
• Shelterin: the protein complex that shapes and safeguards human telomeres. (2005, positive): “In the case of 53BP1, the critical interaction is with the dimethylated form of K79 of histone H3 (Huyen et al. 2004).”
• Chromatin challenges during DNA replication and repair. (2007, neutral): “In addition, reduction of chromatin plasticity may be essential to inactivate the DNA-damage response by inhibiting further recruitment of checkpoint mediators that directly bind to constitutive histone marks, such as H3K79me3 and H4K20me3 (Huyen et al., 2004; Murr et al., 2006; Sanders et al., 2004”
• DNA processing is not required for ATM-mediated telomere damage response after TRF2 deletion (2005, background): “It is possible that t-loops, perhaps aided by telomeric proteins, enforce a nucleosomal organization that resembles the chromatin of intact chromosomal DNA, thus masking the chromosome ends from factors that detect DSBs based on altered chromatin stat”
• The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. (2009, positive): “By contrast, 53BP1 does not possess ubiquitin-binding domains, and its localization to DNA damage sites, rather, depends on its Tudor domain, a methyl-lysine residuebinding module (Botuyan et al., 2006; Huyen et al., 2004).”
• Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications. (2011, background): “2007), while human 53BP1 was initially reported to bind H3K79me3 and subsequently H4K20me1/2 (mono or dimethylated), which might be more physiologically relevant (Huyen et al. 2004; Botuyan et al. 2006; Oda et al. 2010).”
• How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers (2007, background): “Immunofluorescence imaging of cellular distribution showed that mammalian p53-binding protein (53BP1) and its fission yeast homolog Crb2p relocalize to double-strand breaks (DSBs) upon exposure to DNA-damaging agent”
• The role of double-strand break repair — insights from human genetics (2006, background): “Additionally, chromatin relaxation in the vicinity of the DSB has been proposed to expose constitutively methylated lysine residues on histone H3, which facilitates the recruitment of TP53BP1 (Ref”
• The γ‐H2A.X: Is it just a surrogate marker of double‐strand breaks or much more? (2008, background): “Alternatively, it is possible that a kinase other than ATM, ATR, and DNA-Pkcs may be responsible for the formation of these g-H2A.”