Role for RIF1-interacting partner DDX1 in BLM recruitment to DNA double-strand breaks

Li, Lei; Poon, Ho-Yin; Hildebrandt, Matthew R.; Monckton, Elizabeth A.; Germain, Devon R.; Fahlman, Richard P.; Godbout, Roseline

doi:10.1016/j.dnarep.2017.05.001

Cited by 15 publications

(23 citation statements)

References 63 publications

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“…Previously it has been reported that CSB recruitment to DSBs is dependent upon transcription 27 . RNA is reported to mediate 53BP1 and RIF1 recruitment to DSBs 47 , 48 . Perhaps, CSB recruitment by RIF1 to DSBs might also be regulated by transcription, which would require future investigation.…”

Section: Discussionmentioning

confidence: 99%

ATM and CDK2 control chromatin remodeler CSB to inhibit RIF1 in DSB repair pathway choice

et al. 2017

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CSB, a member of the SWI2/SNF2 superfamily, is implicated in DNA double-strand break (DSB) repair. However, how it regulates this repair process is poorly understood. Here we uncover that CSB interacts via its newly identified winged helix domain with RIF1, an effector of 53BP1, and that this interaction mediates CSB recruitment to DSBs in S phase. At DSBs, CSB remodels chromatin by evicting histones, which limits RIF1 and its effector MAD2L2 but promotes BRCA1 accumulation. The chromatin remodeling activity of CSB requires not only damage-induced phosphorylation on S10 by ATM but also cell cycle-dependent phosphorylation on S158 by cyclin A-CDK2. Both modifications modulate the interaction of the CSB N-terminal region with its ATPase domain, the activity of which has been previously reported to be autorepressed by the N-terminal region. These results suggest that ATM and CDK2 control the chromatin remodeling activity of CSB in the regulation of DSB repair pathway choice.

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Section: Discussionmentioning

confidence: 99%

ATM and CDK2 control chromatin remodeler CSB to inhibit RIF1 in DSB repair pathway choice

et al. 2017

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“…Another RNA helicase active at DSBs is DEAD Box 1 (DDX1), which unwinds both RNA:RNA and RNA:DNA hybrids (Chen et al, 2002;Li et al, 2008;Li et al, 2016). DDX1 accumulates at DSBs in an ATM-and 53BP1-dependent manner (Li et al, 2008;Li et al, 2017). At break sites, DDX1 FIGURE 3 | RBPs involved in the regulation of R-loop structures, processing of non-coding RNAs, RNA-templated DNA repair, and phase separation.…”

Section: Rna-binding Protein-rna Interactions Are Central To Double-strand Break Signaling and Repairmentioning

confidence: 99%

New Faces of old Friends: Emerging new Roles of RNA-Binding Proteins in the DNA Double-Strand Break Response

Klaric

Wüst

Panier

2021

Front. Mol. Biosci.

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DNA double-strand breaks (DSBs) are highly cytotoxic DNA lesions. To protect genomic stability and ensure cell homeostasis, cells mount a complex signaling-based response that not only coordinates the repair of the broken DNA strand but also activates cell cycle checkpoints and, if necessary, induces cell death. The last decade has seen a flurry of studies that have identified RNA-binding proteins (RBPs) as novel regulators of the DSB response. While many of these RBPs have well-characterized roles in gene expression, it is becoming increasingly clear that they also have non-canonical functions in the DSB response that go well beyond transcription, splicing and mRNA processing. Here, we review the current understanding of how RBPs are integrated into the cellular response to DSBs and describe how these proteins directly participate in signal transduction, amplification and repair at damaged chromatin. In addition, we discuss the implications of an RBP-mediated DSB response for genome instability and age-associated diseases such as cancer and neurodegeneration.

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“…63,64 DDX1 is phosphorylated by ATM and co-localises with γH2AX rapidly in response to irradiation to facilitate HR. 11,65,66 DHX9 interacts directly with PARP1 and is required for the formation of R-loops. 58,67 Both DHX9 and Senataxin have been shown to reduce chromosomal instability and promote cell survival.…”

Section: The Dna Double-stranded Break Response: An Overviewmentioning

confidence: 99%

The roles of RNA in DNA double-strand break repair

et al. 2020

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Effective DNA repair is essential for cell survival: a failure to correctly repair damage leads to the accumulation of mutations and is the driving force for carcinogenesis. Multiple pathways have evolved to protect against both intrinsic and extrinsic genotoxic events, and recent developments have highlighted an unforeseen critical role for RNA in ensuring genome stability. It is currently unclear exactly how RNA molecules participate in the repair pathways, although many models have been proposed and it is possible that RNA acts in diverse ways to facilitate DNA repair. A number of well-documented DNA repair factors have been described to have RNA-binding capacities and, moreover, screens investigating DNA-damage repair mechanisms have identified RNA-binding proteins as a major group of novel factors involved in DNA repair. In this review, we integrate some of these datasets to identify commonalities that might highlight novel and interesting factors for future investigations. This emerging role for RNA opens up a new dimension in the field of DNA repair; we discuss its impact on our current understanding of DNA repair processes and consider how it might influence cancer progression.

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Role for RIF1-interacting partner DDX1 in BLM recruitment to DNA double-strand breaks

Cited by 15 publications

References 63 publications

ATM and CDK2 control chromatin remodeler CSB to inhibit RIF1 in DSB repair pathway choice

ATM and CDK2 control chromatin remodeler CSB to inhibit RIF1 in DSB repair pathway choice

New Faces of old Friends: Emerging new Roles of RNA-Binding Proteins in the DNA Double-Strand Break Response

The roles of RNA in DNA double-strand break repair

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