HP1α recruitment to DNA damage by p150CAF-1 promotes homologous recombination repair

Baldeyron, Céline; Soria, Gastón; Roche, Danièle; Cook, Adam J. L.; Almouzni, Geneviève

doi:10.1083/jcb.201101030

Cited by 184 publications

(166 citation statements)

References 92 publications

(178 reference statements)

Supporting

Mentioning

139

Contrasting

Order By: Relevance

“…In line with this hypothesis, HP1α knockdown impairs both 53BP1 and BRCA1 recruitment to sites of damage. 17 Given that 53BP1 and BRCA1 have opposite effects on DNA-end resection, [30][31][32][33] further research on this particular issue would certainly be critical to shed light on the molecular details of HP1 role during this process.…”

Section: Discussionmentioning

confidence: 99%

“…To explore how HP1 proteins impact on HR at a molecular level, we considered whether RAD51 loading could be affected due to impaired DNA end resection at the sites of DNA breaks. Such hypothesis is supported by the fact that HP1α knockdown decreases the levels of RPA32 phosphorylation after DNA damage induction with camptothecin, 17 thus suggesting that the processing of single-stranded DNA might be affected. We thus examined the effect of knocking down the different HP1 paralogs on camptothecin-induced RPA32 phosphorylation and foci formation ( Fig.…”

Section: Introductionmentioning

confidence: 92%

“…17 Here, we decided to study HP1α and the other two mammalian paralogs of HP1 (β and γ) under equivalent experimental settings. Initially, using human U2OS cells we set up optimal knockdown conditions for each HP1 paralog (Fig.…”

Section: Hp1 Paralogs Differentially Modulate Homologous Recombinatiomentioning

confidence: 99%

“…In mammalian cells, HP1α knockdown impairs the recruitment of the homologous recombination protein RAD51 to sites of local damage as well as cell survival after ionizing radiation. 17 In contrast, knockdown of the HP1 Drosophila ortholog HP1a does not impair RAD51 recruitment. 18 Intriguingly as well, knocking-out of C. elegans HP1 orthologs (hpl-1 and hpl-2) leads to opposite outcomes on cell survival after ionizing radiation (IR): hpl-1 KO shows increased resistance to IR, while hpl-2 KO is highly sensitive.…”

Section: Introductionmentioning

confidence: 97%

“…2 Following UV irradiation, exposure to α particles, soft X-rays and laser micro-irradiation, mammalian HP1 paralogs show reproducible accumulation at sites of damage. [14][15][16][17] While the mechanism of recruitment to sites of DNA damage for all HP1 paralogs involves their direct interaction with the largest subunit of the chromatin assembly factor 1 (CAF-1), 17 several lines of evidence indicate that their roles might not completely overlap. In mammalian cells, HP1α knockdown impairs the recruitment of the homologous recombination protein RAD51 to sites of local damage as well as cell survival after ionizing radiation.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Differential contribution of HP1 proteins to DNA end resection and homology-directed repair

Soria

Almouzni

2013

Cell Cycle

Self Cite

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 92%

Section: Hp1 Paralogs Differentially Modulate Homologous Recombinatiomentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Differential contribution of HP1 proteins to DNA end resection and homology-directed repair

Soria

Almouzni

2013

Cell Cycle

Self Cite

View full text Add to dashboard Cite

Chromatin modifications during repair of environmental exposure‐induced DNA damage: A potential mechanism for stable epigenetic alterations

O’Hagan

2013

Environ and Mol Mutagen

View full text Add to dashboard Cite

Exposures to environmental toxicants and toxins cause epigenetic changes that likely play a role in the development of diseases associated with exposure. The mechanism behind these exposure-induced epigenetic changes is currently unknown. One commonality between most environmental exposures is that they cause DNA damage either directly or through causing an increase in reactive oxygen species, which can damage DNA. Like transcription, DNA damage repair must occur in the context of chromatin requiring both histone modifications and ATP-dependent chromatin remodeling. These chromatin changes aid in DNA damage accessibility and signaling. Several proteins and complexes involved in epigenetic silencing during both development and cancer have been found to be localized to sites of DNA damage. The chromatin-based response to DNA damage is considered a transient event, with chromatin being restored to normal as DNA damage repair is completed. However, in individuals chronically exposed to environmental toxicants or with chronic inflammatory disease, repeated DNA damage-induced chromatin rearrangement may ultimately lead to permanent epigenetic alterations. Understanding the mechanism behind exposure-induced epigenetic changes will allow us to develop strategies to prevent or reverse these changes. This review focuses on epigenetic changes and DNA damage induced by environmental exposures, the chromatin changes that occur around sites of DNA damage, and how these transient chromatin changes may lead to heritable epigenetic alterations at sites of chronic exposure.

show abstract

Acetylation‐dependent nuclear arrangement and recruitment of BMI1 protein to UV‐damaged chromatin

Šustáčková

Kozubek

Stixová

et al. 2012

Journal Cellular Physiology

View full text Add to dashboard Cite

Polycomb group (PcG) proteins, organized into Polycomb bodies, are important regulatory components of epigenetic processes involved in the heritable transcriptional repression of target genes. Here, we asked whether acetylation can influence the nuclear arrangement and function of the BMI1 protein, a core component of the Polycomb group complex, PRC1. We used time-lapse confocal microscopy, micro-irradiation by UV laser (355 nm) and GFP technology to study the dynamics and function of the BMI1 protein. We observed that BMI1 was recruited to UV-damaged chromatin simultaneously with decreased lysine acetylation, followed by the recruitment of heterochromatin protein HP1β to micro-irradiated regions. Pronounced recruitment of BMI1 was rapid, with half-time τ = 15 sec; thus, BMI1 is likely involved in the initiation step leading to the recognition of UV-damaged sites. Histone hyperacetylation, stimulated by HDAC inhibitor TSA, suppression of transcription by actinomycin D, and ATP-depletion prevented increased accumulation of BMI1 to γH2AX-positive irradiated chromatin. Moreover, BMI1 had slight ability to recognize spontaneously occurring DNA breaks caused by other pathophysiological processes. Taken together, our data indicate that the dynamics of recognition of UV-damaged chromatin, and the nuclear arrangement of BMI1 protein can be influenced by acetylation and occur as an early event prior to the recruitment of HPβ to UV-irradiated chromatin.

show abstract

HP1α recruitment to DNA damage by p150CAF-1 promotes homologous recombination repair

Abstract: p150CAF-1-mediated recruitment of HP1α to DNA is essential for efficient assembly of DNA damage response complexes and subsequent homologous recombination repair.

Cited by 184 publications

References 92 publications

Differential contribution of HP1 proteins to DNA end resection and homology-directed repair

Differential contribution of HP1 proteins to DNA end resection and homology-directed repair

Chromatin modifications during repair of environmental exposure‐induced DNA damage: A potential mechanism for stable epigenetic alterations

Acetylation‐dependent nuclear arrangement and recruitment of BMI1 protein to UV‐damaged chromatin

Contact Info

Product

Resources

About