Tumor suppressor p53 dependent recruitment of nucleotide excision repair factors XPC and TFIIH to DNA damage

Wang, Qi-En; Zhu, Qianzheng; Wani, Mohd Lateef; Wani, Gulzar; Chen, Jianming; Wani, Altaf A.

doi:10.1016/s1568-7864(03)00002-8

Cited by 91 publications

(83 citation statements)

References 44 publications

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“…The XPC protein binds tightly with an HR23B protein to form a stable XPC-HR23B complex [17][18][19]. The XPC protein also interacts with several other important protein components including the basal transcription factor TFIIH and the centrisomal protein CEN2 [18][19][20][21][22]. Recent studies identified the XPC-HR23B complex as the first protein component that recognizes and binds to the damaged sites [23][24][25].…”

Section: Introductionmentioning

confidence: 99%

The involvement of XPC protein in the cisplatin DNA damaging treatment-mediated cellular response

et al. 2004

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Recognition of DNA damage is a critical step for DNA damage-mediated cellular response. XPC is an important DNA damage recognition protein involved in nucleotide excision repair (NER). We have studied the XPC protein in cisplatin DNA damaging treatment-mediated cellular response. Comparison of the microarray data from both normal and XPCdefective human fibroblasts identified 861 XPC-responsive genes in the cisplatin treatment (with minimum fold change>1.5).The cell cycle and cell proliferation-related genes are the most affected genes by the XPC defect in the treatment. Many other cellular function genes, especially the DNA repair and signal transduction-related genes, were also affected by the XPC defect in the treatment. To validate the microarray data, the transcription levels of some microarray-identified genes were also determined by an RT-PCR based real time PCR assay. The real time PCR results are consistent with the microarray data for most of the tested genes, indicating the reliability of the microarray data. To further validate the microarray data, the cisplatin treatment-mediated caspase-3 activation was also determined. The Western blot hybridization results indicate that the XPC defect greatly attenuates the cisplatin treatment-mediated Caspase-3 activation. We elucidated the role of p53 protein in the XPC protein DNA damage recognition-mediated signaling process. The XPC defect reduces the cisplatin treatment-mediated p53 response. These results suggest that the XPC protein plays an important role in the cisplatin treatment-mediated cellular response. It may also suggest a possible mechanism of cancer cell drug resistance.

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Section: Introductionmentioning

confidence: 99%

The involvement of XPC protein in the cisplatin DNA damaging treatment-mediated cellular response

et al. 2004

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“…For localized micropore UV irradiation, OSU-2 cells growing on glass coverslips were washed with PBS and UV irradiated through a 5 M isopore polycarbonate filter (Millipore, Bedford, MA) as described previously (20).…”

Section: Methodsmentioning

confidence: 99%

“…Immunofluorescent Staining-After the desired treatment, OSU-2 cells were fixed with 2% paraformaldehyde in 0.5% Triton X-100 as previously described (20), and double stained with rabbit anti-XPC and mouse anti-CPD antibodies to study the recruitment of XPC to the UV damage site. The cells were also stained with rabbit anti-XPB (Santa Cruz Biotechnology) and mouse anti-CPD antibodies to study the recruitment of XPB to UV lesion.…”

Section: Methodsmentioning

confidence: 99%

Modulation of Nucleotide Excision Repair by Mammalian SWI/SNF Chromatin-remodeling Complex

Zhao

Wang

Ray

et al. 2009

Journal of Biological Chemistry

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Accessibility within chromatin is an important factor in the prompt removal of UV-induced DNA damage by nucleotide excision repair (NER). Chromatin remodeling by the SWI/SNF complex has been shown to play an important modulating role in NER in vitro and yeast in vivo. Nevertheless, the molecular basis of cross-talk between SWI/SNF and NER in mammalian cells is not fully understood. Here, we show that knockdown of Brg1, the ATPase subunit of SWI/SNF, negatively affects the elimination of cyclobutane pyrimidine dimers (CPD), but not of pyrimidine (6, 4)pyrimidone photoproducts (6-4PP) following UV irradiation of mammalian cells. Brg1-deficient cells exhibit a lower chromatin relaxation as well as impaired recruitment of downstream NER factors, XPG and PCNA, to UV lesions. However, the assembly of upstream NER factors, DDB2 and XPC, at the damage site was unaffected by Brg1 knockdown. Interestingly, Brg1 interacts with XPC within chromatin and is recruited to UV-damaged sites in a DDB2-and XPC-dependent manner. Also, postirradiation decrease of XPC levels occurred more rapidly in Brg1-deficient than normal cells. Conversely, XPC transcription remained unaltered upon Brg1 knockdown indicating that Brg1 affects the stability of XPC protein following irradiation. Thus, Brg1 facilitates different stages of NER by initially modulating UV-induced chromatin relaxation and stabilizing XPC at the damage sites, and subsequently stimulating the recruitment of XPG and PCNA to successfully culminate the repair.

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“…Localized Micropore UV Irradiation and Immunofluorescent Staining-OSU-2 cells growing on glass coverslips were pretreated with either SB203580 or DMSO for 30 min, and the cells were then washed with phosphate-buffered saline and UV-irradiated through a 5-m isopore polycarbonate filter (Millipore, Bedford, MA) as described previously (47). The cells were then double stained with rabbit anti-XPC and mouse anti-CPD (TDM-2, MBL International Corporation), or rabbit anti-XPB and mouse anti-CPD, or rabbit-anti-phospho-p38 and mouse anti-CPD antibodies.…”

Section: Methodsmentioning

confidence: 99%

The p38 Mitogen-activated Protein Kinase Augments Nucleotide Excision Repair by Mediating DDB2 Degradation and Chromatin Relaxation

Zhao

Barakat

Qin

et al. 2008

Journal of Biological Chemistry

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The p38 MAPK is a family of serine/threonine protein kinases that play important roles in cellular responses to external stress signals, e.g. UV irradiation. To assess the role of p38 MAPK pathway in nucleotide excision repair (NER), the most versatile DNA repair pathway, we determined the efficiency of NER in cells treated with p38 MAPK inhibitor SB203580 and found that p38 MAPK is required for the prompt repair of UV-induced DNA damage CPD. We further investigated the possible mechanism through which p38 MAPK regulates NER and found that p38 MAPK mediates UV-induced histone H3 acetylation and chromatin relaxation. Moreover, p38 MAPK also regulates UVinduced DDB2 ubiquitylation and degradation via phosphorylation of the target protein. Finally, our results showed that p38 MAPK is required for the recruitment of NER factors XPC and TFIIH to UV-induced DNA damage sites. We conclude that p38 MAPK regulates chromatin remodeling as well as DDB2 degradation for facilitating NER factor assembly.

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Tumor suppressor p53 dependent recruitment of nucleotide excision repair factors XPC and TFIIH to DNA damage

Cited by 91 publications

References 44 publications

The involvement of XPC protein in the cisplatin DNA damaging treatment-mediated cellular response

The involvement of XPC protein in the cisplatin DNA damaging treatment-mediated cellular response

Modulation of Nucleotide Excision Repair by Mammalian SWI/SNF Chromatin-remodeling Complex

The p38 Mitogen-activated Protein Kinase Augments Nucleotide Excision Repair by Mediating DDB2 Degradation and Chromatin Relaxation

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