The involvement of ataxia-telangiectasia mutated protein activation in nucleotide excision repair-facilitated cell survival with cisplatin treatment

Colton, Stephanie L.; Xu, Xiaoxin S.; Wang, Y. Alan; Wang, Gan

doi:10.1074/jbc.m602826200

Cited by 65DNA Repair MechanismsMetal complexes synthesis and propertiesCell death mechanisms and regulation

The involvement of ataxia-telangiectasia mutated protein activation in nucleotide excision repair-facilitated cell survival with cisplatin treatment

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Colton, Stephanie L., Xu, Xiaoxin S., Wang, Y. Alan, Wang, Gan·2006·Journal of Biological Chemistry

DOI 10.1074/jbc.m602826200

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Abstract

DNA damage can lead to either DNA repair with cell survival or to apoptotic cell death. Although the biochemical processes underlying DNA repair and apoptosis have been extensively studied, the mechanisms by which cells determine whether the damage will be repaired or the apoptotic pathway will be activated is largely unknown. We have studied the role of nucleotide excision repair (NER) in cisplatin DNA damage-induced apoptotic cell death using both normal human fibroblasts and NER-defective xeroderma pigmentosum (XP) XPA and XPG cells. The caspase-3 activation experiment demonstrated a greatly increased casapse-3 activation in the NER-defective cells following cisplatin treatment. The flow cytometry experiment revealed an altered cell cycle arrest pattern of the NER-defective cells following cisplatin treatment. The results obtained from the Western blot experiment showed that NER defects resulted in enhanced CHK1 phosphorylation and p21 induction after cisplatin treatment. The cisplatin treatment-induced ATM phosphorylation, however, was attenuated in NER-defective cells. The results obtained from our immunoprecipitation experiment further demonstrated that the ATM protein interacted with the TFIIH basal transcription factor and the XPG protein of the NER pathway. It also showed that a functional XPC protein was required for the association of the ATM protein to genomic DNA. These results suggest that the NER process may prevent the cisplatin treatment-induced apoptosis by activating the ATM protein, and that the presence of the XPC protein is essential for recruiting the ATM protein to the DNA template.

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After cisplatin treatment, XPC physically interacts with ATM and participates in ATM activation.
“Furthermore, in response to cisplatin treatment, XPC physically interacts with ATM, and is involved in ATM activation [42].”
From NER initiation factors, DDB2 and XPC, regulate UV radiation response by recruiting ATR and ATM kinases to DNA damage sites (2013) · cites this paper as [42]
NER plays a role in ATM activation after cisplatin treatment; ATM physically interacts with NER factors and this association is required for ATM recruitment to DNA.
“In addition, a role for NER in the activation of ATM after cisplatin treatment was discovered. Immunoprecipitation experiments revealed a physical interaction between ATM and NER factors and this association is required for ATM recruitment to DNA [94] (Fig. 3).”
From Mind the gap: keeping UV lesions in check (2011) · cites this paper as [94]
XPC and XPG are required for ATM recruitment to damage sites after cisplatin treatment, which prevents cisplatin-induced apoptosis.
“XPC and XPG are essential for the recruitment of ATM to damage sites after cisplatin treatment, preventing cisplatin-induced apoptosis [204]”
From Functional interplay between ATM/ATR-mediated DNA damage response and DNA repair pathways in oxidative stress (2014) · cites this paper as [204]

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The involvement of ataxia-telangiectasia mutated protein activation in nucleotide excision repair-facilitated cell survival with cisplatin treatment. VOLUME 281 (2006) PAGES 27117-27125
Colton, S. L., Xu, X., Wang, Y., & Gan, W. (2007) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)33756-1
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Authors: Colton, S. L., Xu, X. S., Wang, Y. A., & Wang, G.
Affiliations: Wayne State University (US)
Corresponding author: Wang, Gan
ORCID: Wang, Y. Alan
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2006-09
Volume: 281
Issue: 37
Pages: 27117-27125
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m602826200
OpenAlex: W1974533828
Cited by: 65
References: 74
Citations by year: 2024: 4 · 2023: 5 · 2022: 4 · 2021: 1 · 2020: 1 · 2019: 5 · 2018: 2 · 2016: 2 · 2015: 8 · 2014: 3 · 2013: 4 · 2012: 3
FWCI: 1.88
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5168 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: Wayne State University
National Institutes of Health (5p30es006639-15, ES06639, P30 ES06639)
National Institute of Environmental Health Sciences (P-30-ES06639, T32ES01216, R01ES009699)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Health Sciences › Medicine › Oncology › Metal complexes synthesis and properties
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Keywords: ATM, nucleotide excision repair, cisplatin, apoptosis, xeroderma pigmentosum, XPA, XPG, XPC, caspase-3 activation, cell cycle arrest, Chk1 phosphorylation, p21, TFIIH, DNA damage response
MeSH terms: Checkpoint Kinase 1, Antineoplastic Agents, Cell Survival, Cisplatin, DNA Damage, DNA Repair, DNA-Binding Proteins, Enzyme Activation, Fibroblasts, Humans, Nucleotides, Phosphorylation, Protein Kinases, Apoptosis, Protein Serine-Threonine Kinases, Cell Cycle Proteins, Caspases, Tumor Suppressor Proteins, Caspase 3, Ataxia Telangiectasia Mutated Proteins

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The involvement of ataxia-telangiectasia mutated protein activation in nucleotide excision repair-facilitated cell survival with cisplatin treatment

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