A neomorphic cancer cell-specific role of MAGE-A4 in trans-lesion synthesis

Trans-lesion synthesis (TLS) is an important DNA-damage tolerance mechanism that permits ongoing DNA synthesis in cells harbouring damaged genomes. The E3 ubiquitin ligase RAD18 activates TLS by promoting recruitment of Y-family DNA polymerases to sites of DNA-damage-induced replication fork stallin...

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Published inNature communications Vol. 7; no. 1; pp. 12105 - 14
Main Authors Gao, Yanzhe, Mutter-Rottmayer, Elizabeth, Greenwalt, Alicia M., Goldfarb, Dennis, Yan, Feng, Yang, Yang, Martinez-Chacin, Raquel C., Pearce, Kenneth H., Tateishi, Satoshi, Major, Michael B., Vaziri, Cyrus
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 05.07.2016
Nature Publishing Group
Nature Portfolio
Subjects
631/337/1427
631/337/474/2073
631/80/86
A549 Cells
Animals
Antigens
Antigens, Neoplasm - genetics
Antigens, Neoplasm - metabolism
Biology
Cancer
Cell cycle
Cell Line
Cell Line, Tumor
Chemical synthesis
Cloning, Molecular
Curricula
Damage detection
Damage tolerance
Deoxyribonucleic acid
Depletion
DNA
DNA biosynthesis
DNA Damage
DNA polymerase
DNA Repair
DNA Replication
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
DNA-directed DNA polymerase
Ectopic expression
Escherichia coli - genetics
Escherichia coli - metabolism
Fibroblasts - cytology
Fibroblasts - metabolism
Fibroblasts - radiation effects
Gene Expression Regulation, Neoplastic
Genetic Vectors - chemistry
Genetic Vectors - metabolism
Genomes
Genotoxicity
HCT116 Cells
HeLa Cells
Histones - genetics
Histones - metabolism
Humanities and Social Sciences
Humans
Immunological tolerance
Irradiation
Lesions
Melanoma
Mice
multidisciplinary
Mutagenesis
Mutation
Neoplasm Proteins - genetics
Neoplasm Proteins - metabolism
Protein biosynthesis
Radiation damage
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Replication
Science
Science (multidisciplinary)
Signal Transduction
Skin cancer
Ubiquitin-Conjugating Enzymes - genetics
Ubiquitin-Conjugating Enzymes - metabolism
Ubiquitin-protein ligase
Ubiquitin-Protein Ligases - genetics
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
Ultraviolet radiation
Ultraviolet Rays
North Carolina
United States > US
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Abstract Trans-lesion synthesis (TLS) is an important DNA-damage tolerance mechanism that permits ongoing DNA synthesis in cells harbouring damaged genomes. The E3 ubiquitin ligase RAD18 activates TLS by promoting recruitment of Y-family DNA polymerases to sites of DNA-damage-induced replication fork stalling. Here we identify the cancer/testes antigen melanoma antigen-A4 (MAGE-A4) as a tumour cell-specific RAD18-binding partner and an activator of TLS. MAGE-A4 depletion from MAGE-A4-expressing cancer cells destabilizes RAD18. Conversely, ectopic expression of MAGE-A4 (in cell lines lacking endogenous MAGE-A4) promotes RAD18 stability. DNA-damage-induced mono-ubiquitination of the RAD18 substrate PCNA is attenuated by MAGE-A4 silencing. MAGE-A4-depleted cells fail to resume DNA synthesis normally following ultraviolet irradiation and accumulate γH2AX, thereby recapitulating major hallmarks of TLS deficiency. Taken together, these results demonstrate a mechanism by which reprogramming of ubiquitin signalling in cancer cells can influence DNA damage tolerance and probably contribute to an altered genomic landscape. RAD18 is an important protein in trans-lesion synthesis, an error-prone damage-tolerant mode of DNA replication. Here the authors show that MAGE-A4 stabilizes RAD18 and allows cancer cells to maintain on-going DNA synthesis in the face of genotoxic injury.
AbstractList Abstract Trans-lesion synthesis (TLS) is an important DNA-damage tolerance mechanism that permits ongoing DNA synthesis in cells harbouring damaged genomes. The E3 ubiquitin ligase RAD18 activates TLS by promoting recruitment of Y-family DNA polymerases to sites of DNA-damage-induced replication fork stalling. Here we identify the cancer/testes antigen melanoma antigen-A4 (MAGE-A4) as a tumour cell-specific RAD18-binding partner and an activator of TLS. MAGE-A4 depletion from MAGE-A4-expressing cancer cells destabilizes RAD18. Conversely, ectopic expression of MAGE-A4 (in cell lines lacking endogenous MAGE-A4) promotes RAD18 stability. DNA-damage-induced mono-ubiquitination of the RAD18 substrate PCNA is attenuated by MAGE-A4 silencing. MAGE-A4-depleted cells fail to resume DNA synthesis normally following ultraviolet irradiation and accumulate γH2AX, thereby recapitulating major hallmarks of TLS deficiency. Taken together, these results demonstrate a mechanism by which reprogramming of ubiquitin signalling in cancer cells can influence DNA damage tolerance and probably contribute to an altered genomic landscape.
Trans-lesion synthesis (TLS) is an important DNA-damage tolerance mechanism that permits ongoing DNA synthesis in cells harbouring damaged genomes. The E3 ubiquitin ligase RAD18 activates TLS by promoting recruitment of Y-family DNA polymerases to sites of DNA-damage-induced replication fork stalling. Here we identify the cancer/testes antigen melanoma antigen-A4 (MAGE-A4) as a tumour cell-specific RAD18-binding partner and an activator of TLS. MAGE-A4 depletion from MAGE-A4-expressing cancer cells destabilizes RAD18. Conversely, ectopic expression of MAGE-A4 (in cell lines lacking endogenous MAGE-A4) promotes RAD18 stability. DNA-damage-induced mono-ubiquitination of the RAD18 substrate PCNA is attenuated by MAGE-A4 silencing. MAGE-A4-depleted cells fail to resume DNA synthesis normally following ultraviolet irradiation and accumulate γH2AX, thereby recapitulating major hallmarks of TLS deficiency. Taken together, these results demonstrate a mechanism by which reprogramming of ubiquitin signalling in cancer cells can influence DNA damage tolerance and probably contribute to an altered genomic landscape.
Trans-lesion synthesis (TLS) is an important DNA-damage tolerance mechanism that permits ongoing DNA synthesis in cells harbouring damaged genomes. The E3 ubiquitin ligase RAD18 activates TLS by promoting recruitment of Y-family DNA polymerases to sites of DNA-damage-induced replication fork stalling. Here we identify the cancer/testes antigen melanoma antigen-A4 (MAGE-A4) as a tumour cell-specific RAD18-binding partner and an activator of TLS. MAGE-A4 depletion from MAGE-A4-expressing cancer cells destabilizes RAD18. Conversely, ectopic expression of MAGE-A4 (in cell lines lacking endogenous MAGE-A4) promotes RAD18 stability. DNA-damage-induced mono-ubiquitination of the RAD18 substrate PCNA is attenuated by MAGE-A4 silencing. MAGE-A4-depleted cells fail to resume DNA synthesis normally following ultraviolet irradiation and accumulate γH2AX, thereby recapitulating major hallmarks of TLS deficiency. Taken together, these results demonstrate a mechanism by which reprogramming of ubiquitin signalling in cancer cells can influence DNA damage tolerance and probably contribute to an altered genomic landscape.Trans-lesion synthesis (TLS) is an important DNA-damage tolerance mechanism that permits ongoing DNA synthesis in cells harbouring damaged genomes. The E3 ubiquitin ligase RAD18 activates TLS by promoting recruitment of Y-family DNA polymerases to sites of DNA-damage-induced replication fork stalling. Here we identify the cancer/testes antigen melanoma antigen-A4 (MAGE-A4) as a tumour cell-specific RAD18-binding partner and an activator of TLS. MAGE-A4 depletion from MAGE-A4-expressing cancer cells destabilizes RAD18. Conversely, ectopic expression of MAGE-A4 (in cell lines lacking endogenous MAGE-A4) promotes RAD18 stability. DNA-damage-induced mono-ubiquitination of the RAD18 substrate PCNA is attenuated by MAGE-A4 silencing. MAGE-A4-depleted cells fail to resume DNA synthesis normally following ultraviolet irradiation and accumulate γH2AX, thereby recapitulating major hallmarks of TLS deficiency. Taken together, these results demonstrate a mechanism by which reprogramming of ubiquitin signalling in cancer cells can influence DNA damage tolerance and probably contribute to an altered genomic landscape.
Trans-lesion synthesis (TLS) is an important DNA-damage tolerance mechanism that permits ongoing DNA synthesis in cells harbouring damaged genomes. The E3 ubiquitin ligase RAD18 activates TLS by promoting recruitment of Y-family DNA polymerases to sites of DNA-damage-induced replication fork stalling. Here we identify the cancer/testes antigen melanoma antigen-A4 (MAGE-A4) as a tumour cell-specific RAD18-binding partner and an activator of TLS. MAGE-A4 depletion from MAGE-A4-expressing cancer cells destabilizes RAD18. Conversely, ectopic expression of MAGE-A4 (in cell lines lacking endogenous MAGE-A4) promotes RAD18 stability. DNA-damage-induced mono-ubiquitination of the RAD18 substrate PCNA is attenuated by MAGE-A4 silencing. MAGE-A4-depleted cells fail to resume DNA synthesis normally following ultraviolet irradiation and accumulate γH2AX, thereby recapitulating major hallmarks of TLS deficiency. Taken together, these results demonstrate a mechanism by which reprogramming of ubiquitin signalling in cancer cells can influence DNA damage tolerance and probably contribute to an altered genomic landscape. RAD18 is an important protein in trans-lesion synthesis, an error-prone damage-tolerant mode of DNA replication. Here the authors show that MAGE-A4 stabilizes RAD18 and allows cancer cells to maintain on-going DNA synthesis in the face of genotoxic injury.
Trans-lesion synthesis (TLS) is an important DNA-damage tolerance mechanism that permits ongoing DNA synthesis in cells harbouring damaged genomes. The E3 ubiquitin ligase RAD18 activates TLS by promoting recruitment of Y-family DNA polymerases to sites of DNA-damage-induced replication fork stalling. Here we identify the cancer/testes antigen melanoma antigen-A4 (MAGE-A4) as a tumour cell-specific RAD18-binding partner and an activator of TLS. MAGE-A4 depletion from MAGE-A4-expressing cancer cells destabilizes RAD18. Conversely, ectopic expression of MAGE-A4 (in cell lines lacking endogenous MAGE-A4) promotes RAD18 stability. DNA-damage-induced mono-ubiquitination of the RAD18 substrate PCNA is attenuated by MAGE-A4 silencing. MAGE-A4-depleted cells fail to resume DNA synthesis normally following ultraviolet irradiation and accumulate γH2AX, thereby recapitulating major hallmarks of TLS deficiency. Taken together, these results demonstrate a mechanism by which reprogramming of ubiquitin signalling in cancer cells can influence DNA damage tolerance and probably contribute to an altered genomic landscape.RAD18 is an important protein in trans-lesion synthesis, an error-prone damage-tolerant mode of DNA replication. Here the authors show that MAGE-A4 stabilizes RAD18 and allows cancer cells to maintain on-going DNA synthesis in the face of genotoxic injury.
ArticleNumber 12105
Author Yan, Feng
Tateishi, Satoshi
Greenwalt, Alicia M.
Major, Michael B.
Mutter-Rottmayer, Elizabeth
Gao, Yanzhe
Martinez-Chacin, Raquel C.
Pearce, Kenneth H.
Yang, Yang
Vaziri, Cyrus
Goldfarb, Dennis
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  surname: Mutter-Rottmayer
  fullname: Mutter-Rottmayer, Elizabeth
  organization: Department of Pathology and Laboratory Medicine, University of North Carolina at Chapel Hill, Curriculum in Toxicology, University of North Carolina at Chapel Hill
– sequence: 3
  givenname: Alicia M.
  surname: Greenwalt
  fullname: Greenwalt, Alicia M.
  organization: Department of Pathology and Laboratory Medicine, University of North Carolina at Chapel Hill, Curriculum in Genetics and Molecular Biology, University of North Carolina
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  fullname: Yan, Feng
  organization: Department of Cell Biology and Physiology, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill
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  organization: Department of Pathology and Laboratory Medicine, University of North Carolina at Chapel Hill
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  givenname: Kenneth H.
  surname: Pearce
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/27377895$$D View this record in MEDLINE/PubMed
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SSID ssj0000391844
Score 2.4715207
Snippet Trans-lesion synthesis (TLS) is an important DNA-damage tolerance mechanism that permits ongoing DNA synthesis in cells harbouring damaged genomes. The E3...
Abstract Trans-lesion synthesis (TLS) is an important DNA-damage tolerance mechanism that permits ongoing DNA synthesis in cells harbouring damaged genomes....
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proquest
crossref
pubmed
springer
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 12105
SubjectTerms 631/337/1427
631/337/474/2073
631/80/86
A549 Cells
Animals
Antigens
Antigens, Neoplasm - genetics
Antigens, Neoplasm - metabolism
Biology
Cancer
Cell cycle
Cell Line
Cell Line, Tumor
Chemical synthesis
Cloning, Molecular
Curricula
Damage detection
Damage tolerance
Deoxyribonucleic acid
Depletion
DNA
DNA biosynthesis
DNA Damage
DNA polymerase
DNA Repair
DNA Replication
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
DNA-directed DNA polymerase
Ectopic expression
Escherichia coli - genetics
Escherichia coli - metabolism
Fibroblasts - cytology
Fibroblasts - metabolism
Fibroblasts - radiation effects
Gene Expression Regulation, Neoplastic
Genetic Vectors - chemistry
Genetic Vectors - metabolism
Genomes
Genotoxicity
HCT116 Cells
HeLa Cells
Histones - genetics
Histones - metabolism
Humanities and Social Sciences
Humans
Immunological tolerance
Irradiation
Lesions
Melanoma
Mice
multidisciplinary
Mutagenesis
Mutation
Neoplasm Proteins - genetics
Neoplasm Proteins - metabolism
Protein biosynthesis
Radiation damage
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Replication
Science
Science (multidisciplinary)
Signal Transduction
Skin cancer
Ubiquitin-Conjugating Enzymes - genetics
Ubiquitin-Conjugating Enzymes - metabolism
Ubiquitin-protein ligase
Ubiquitin-Protein Ligases - genetics
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
Ultraviolet radiation
Ultraviolet Rays
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Title A neomorphic cancer cell-specific role of MAGE-A4 in trans-lesion synthesis
URI https://link.springer.com/article/10.1038/ncomms12105
https://www.ncbi.nlm.nih.gov/pubmed/27377895
https://www.proquest.com/docview/1801620979
https://www.proquest.com/docview/3128448955
https://www.proquest.com/docview/1802743872
https://pubmed.ncbi.nlm.nih.gov/PMC4935975
https://doaj.org/article/0e5d0907f6a14928a23a27cda5802f8e
Volume 7
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