SLFN11 inhibits checkpoint maintenance and homologous recombination repair
High expression levels of SLFN11 correlate with the sensitivity of human cancer cells to DNA‐damaging agents. However, little is known about the underlying mechanism. Here, we show that SLFN11 interacts directly with RPA1 and is recruited to sites of DNA damage in an RPA1‐dependent manner. Furthermo...
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| Published in | EMBO reports Vol. 17; no. 1; pp. 94 - 109 |
|---|---|
| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Blackwell Publishing Ltd
01.01.2016
Nature Publishing Group UK Springer Nature B.V John Wiley and Sons Inc |
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| Online Access | Get full text |
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| Abstract | High expression levels of SLFN11 correlate with the sensitivity of human cancer cells to DNA‐damaging agents. However, little is known about the underlying mechanism. Here, we show that SLFN11 interacts directly with RPA1 and is recruited to sites of DNA damage in an RPA1‐dependent manner. Furthermore, we establish that SLFN11 inhibits checkpoint maintenance and homologous recombination repair by promoting the destabilization of the RPA–ssDNA complex, thereby sensitizing cancer cell lines expressing high endogenous levels of SLFN11 to DNA‐damaging agents. Finally, we demonstrate that the RPA1‐binding ability of SLFN11 is required for its function in the DNA damage response. Our findings not only provide novel insight into the molecular mechanisms underlying the drug sensitivity of cancer cell lines expressing SLFN11 at high levels, but also suggest that SLFN11 expression can serve as a biomarker to predict responses to DNA‐damaging therapeutic agents.
Synopsis
High levels of SLFN11 sensitize cancer cell lines to DNA‐damaging agents by inhibiting checkpoint maintenance and homologous recombination repair. SLFN11 expression might serve as a biomarker to predict responses to DNA‐damaging therapeutic agents.
SLFN11 is a DNA damage responsive protein and forms a complex with RPA.
SLFN11 inhibits checkpoint maintenance and homologous recombination repair by destabilizing the RPA–ssDNA complex.
The role of SLFN11 in sensitizing cancer cells to DNA‐damaging agents depends on a physical protein–protein interaction between SLFN11 and RPA1.
Graphical Abstract
High levels of SLFN11 sensitize cancer cell lines to DNA‐damaging agents by inhibiting checkpoint maintenance and homologous recombination repair. SLFN11 expression might serve as a biomarker to predict responses to DNA‐damaging therapeutic agents. |
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| AbstractList | High expression levels of SLFN11 correlate with the sensitivity of human cancer cells to DNA‐damaging agents. However, little is known about the underlying mechanism. Here, we show that SLFN11 interacts directly with RPA1 and is recruited to sites of DNA damage in an RPA1‐dependent manner. Furthermore, we establish that SLFN11 inhibits checkpoint maintenance and homologous recombination repair by promoting the destabilization of the RPA–ssDNA complex, thereby sensitizing cancer cell lines expressing high endogenous levels of SLFN11 to DNA‐damaging agents. Finally, we demonstrate that the RPA1‐binding ability of SLFN11 is required for its function in the DNA damage response. Our findings not only provide novel insight into the molecular mechanisms underlying the drug sensitivity of cancer cell lines expressing SLFN11 at high levels, but also suggest that SLFN11 expression can serve as a biomarker to predict responses to DNA‐damaging therapeutic agents.
Synopsis
High levels of SLFN11 sensitize cancer cell lines to DNA‐damaging agents by inhibiting checkpoint maintenance and homologous recombination repair. SLFN11 expression might serve as a biomarker to predict responses to DNA‐damaging therapeutic agents.
SLFN11 is a DNA damage responsive protein and forms a complex with RPA.
SLFN11 inhibits checkpoint maintenance and homologous recombination repair by destabilizing the RPA–ssDNA complex.
The role of SLFN11 in sensitizing cancer cells to DNA‐damaging agents depends on a physical protein–protein interaction between SLFN11 and RPA1.
Graphical Abstract
High levels of SLFN11 sensitize cancer cell lines to DNA‐damaging agents by inhibiting checkpoint maintenance and homologous recombination repair. SLFN11 expression might serve as a biomarker to predict responses to DNA‐damaging therapeutic agents. High expression levels of SLFN11 correlate with the sensitivity of human cancer cells to DNA‐damaging agents. However, little is known about the underlying mechanism. Here, we show that SLFN11 interacts directly with RPA1 and is recruited to sites of DNA damage in an RPA1‐dependent manner. Furthermore, we establish that SLFN11 inhibits checkpoint maintenance and homologous recombination repair by promoting the destabilization of the RPA–ssDNA complex, thereby sensitizing cancer cell lines expressing high endogenous levels of SLFN11 to DNA‐damaging agents. Finally, we demonstrate that the RPA1‐binding ability of SLFN11 is required for its function in the DNA damage response. Our findings not only provide novel insight into the molecular mechanisms underlying the drug sensitivity of cancer cell lines expressing SLFN11 at high levels, but also suggest that SLFN11 expression can serve as a biomarker to predict responses to DNA‐damaging therapeutic agents. Synopsis High levels of SLFN11 sensitize cancer cell lines to DNA‐damaging agents by inhibiting checkpoint maintenance and homologous recombination repair. SLFN11 expression might serve as a biomarker to predict responses to DNA‐damaging therapeutic agents. SLFN11 is a DNA damage responsive protein and forms a complex with RPA. SLFN11 inhibits checkpoint maintenance and homologous recombination repair by destabilizing the RPA–ssDNA complex. The role of SLFN11 in sensitizing cancer cells to DNA‐damaging agents depends on a physical protein–protein interaction between SLFN11 and RPA1. High levels of SLFN11 sensitize cancer cell lines to DNA‐damaging agents by inhibiting checkpoint maintenance and homologous recombination repair. SLFN11 expression might serve as a biomarker to predict responses to DNA‐damaging therapeutic agents. High expression levels of SLFN11 correlate with the sensitivity of human cancer cells to DNA-damaging agents. However, little is known about the underlying mechanism. Here, we show that SLFN11 interacts directly with RPA1 and is recruited to sites of DNA damage in an RPA1-dependent manner. Furthermore, we establish that SLFN11 inhibits checkpoint maintenance and homologous recombination repair by promoting the destabilization of the RPA-ssDNA complex, thereby sensitizing cancer cell lines expressing high endogenous levels of SLFN11 to DNA-damaging agents. Finally, we demonstrate that the RPA1-binding ability of SLFN11 is required for its function in the DNA damage response. Our findings not only provide novel insight into the molecular mechanisms underlying the drug sensitivity of cancer cell lines expressing SLFN11 at high levels, but also suggest that SLFN11 expression can serve as a biomarker to predict responses to DNA-damaging therapeutic agents. Synopsis High levels of SLFN11 sensitize cancer cell lines to DNA-damaging agents by inhibiting checkpoint maintenance and homologous recombination repair. SLFN11 expression might serve as a biomarker to predict responses to DNA-damaging therapeutic agents. SLFN11 is a DNA damage responsive protein and forms a complex with RPA. SLFN11 inhibits checkpoint maintenance and homologous recombination repair by destabilizing the RPA-ssDNA complex. The role of SLFN11 in sensitizing cancer cells to DNA-damaging agents depends on a physical protein-protein interaction between SLFN11 and RPA1. High expression levels of SLFN11 correlate with the sensitivity of human cancer cells to DNA-damaging agents. However, little is known about the underlying mechanism. Here, we show that SLFN11 interacts directly with RPA1 and is recruited to sites of DNA damage in an RPA1-dependent manner. Furthermore, we establish that SLFN11 inhibits checkpoint maintenance and homologous recombination repair by promoting the destabilization of the RPA-ssDNA complex, thereby sensitizing cancer cell lines expressing high endogenous levels of SLFN11 to DNA-damaging agents. Finally, we demonstrate that the RPA1-binding ability of SLFN11 is required for its function in the DNA damage response. Our findings not only provide novel insight into the molecular mechanisms underlying the drug sensitivity of cancer cell lines expressing SLFN11 at high levels, but also suggest that SLFN11 expression can serve as a biomarker to predict responses to DNA-damaging therapeutic agents.High expression levels of SLFN11 correlate with the sensitivity of human cancer cells to DNA-damaging agents. However, little is known about the underlying mechanism. Here, we show that SLFN11 interacts directly with RPA1 and is recruited to sites of DNA damage in an RPA1-dependent manner. Furthermore, we establish that SLFN11 inhibits checkpoint maintenance and homologous recombination repair by promoting the destabilization of the RPA-ssDNA complex, thereby sensitizing cancer cell lines expressing high endogenous levels of SLFN11 to DNA-damaging agents. Finally, we demonstrate that the RPA1-binding ability of SLFN11 is required for its function in the DNA damage response. Our findings not only provide novel insight into the molecular mechanisms underlying the drug sensitivity of cancer cell lines expressing SLFN11 at high levels, but also suggest that SLFN11 expression can serve as a biomarker to predict responses to DNA-damaging therapeutic agents. High expression levels of SLFN11 correlate with the sensitivity of human cancer cells to DNA-damaging agents. However, little is known about the underlying mechanism. Here, we show that SLFN11 interacts directly with RPA1 and is recruited to sites of DNA damage in an RPA1-dependent manner. Furthermore, we establish that SLFN11 inhibits checkpoint maintenance and homologous recombination repair by promoting the destabilization of the RPA-ssDNA complex, thereby sensitizing cancer cell lines expressing high endogenous levels of SLFN11 to DNA-damaging agents. Finally, we demonstrate that the RPA1-binding ability of SLFN11 is required for its function in the DNA damage response. Our findings not only provide novel insight into the molecular mechanisms underlying the drug sensitivity of cancer cell lines expressing SLFN11 at high levels, but also suggest that SLFN11 expression can serve as a biomarker to predict responses to DNA-damaging therapeutic agents. High expression levels of SLFN 11 correlate with the sensitivity of human cancer cells to DNA ‐damaging agents. However, little is known about the underlying mechanism. Here, we show that SLFN 11 interacts directly with RPA 1 and is recruited to sites of DNA damage in an RPA 1‐dependent manner. Furthermore, we establish that SLFN 11 inhibits checkpoint maintenance and homologous recombination repair by promoting the destabilization of the RPA –ss DNA complex, thereby sensitizing cancer cell lines expressing high endogenous levels of SLFN 11 to DNA ‐damaging agents. Finally, we demonstrate that the RPA 1‐binding ability of SLFN 11 is required for its function in the DNA damage response. Our findings not only provide novel insight into the molecular mechanisms underlying the drug sensitivity of cancer cell lines expressing SLFN 11 at high levels, but also suggest that SLFN 11 expression can serve as a biomarker to predict responses to DNA ‐damaging therapeutic agents. |
| Author | Mu, Yanhua Srivastava, Mrinal Chen, Junjie Lou, Jiangman Zhao, Bin Feng, Xin‐hua Huang, Jun Liu, Ting |
| AuthorAffiliation | 1 Life Sciences Institute and Innovation Center for Cell Signaling Network Zhejiang University Hangzhou Zhejiang China 3 Department of Cell Biology Zhejiang University School of Medicine Hangzhou Zhejiang China 2 Department of Experimental Radiation Oncology University of Texas M.D. Anderson Cancer Center Houston TX USA |
| AuthorAffiliation_xml | – name: 2 Department of Experimental Radiation Oncology University of Texas M.D. Anderson Cancer Center Houston TX USA – name: 3 Department of Cell Biology Zhejiang University School of Medicine Hangzhou Zhejiang China – name: 1 Life Sciences Institute and Innovation Center for Cell Signaling Network Zhejiang University Hangzhou Zhejiang China |
| Author_xml | – sequence: 1 givenname: Yanhua surname: Mu fullname: Mu, Yanhua organization: Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, HangzhouZhejiang, China – sequence: 2 givenname: Jiangman surname: Lou fullname: Lou, Jiangman organization: Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, HangzhouZhejiang, China – sequence: 3 givenname: Mrinal surname: Srivastava fullname: Srivastava, Mrinal organization: Department of Experimental Radiation Oncology, University of Texas M.D. Anderson Cancer Center, TX, Houston, USA – sequence: 4 givenname: Bin surname: Zhao fullname: Zhao, Bin organization: Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, HangzhouZhejiang, China – sequence: 5 givenname: Xin-hua surname: Feng fullname: Feng, Xin-hua organization: Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, HangzhouZhejiang, China – sequence: 6 givenname: Ting surname: Liu fullname: Liu, Ting email: Corresponding author. Tel: +86 571 8898 1376; , liuting518@zju.edu.cn, Corresponding author. Tel: +1 713 792 4863; , jchen8@mdanderson.org, Corresponding author. Tel: +86 571 8898 1391; , jhuang@zju.edu.cn organization: Department of Cell Biology, Zhejiang University School of Medicine, HangzhouZhejiang, China – sequence: 7 givenname: Junjie surname: Chen fullname: Chen, Junjie email: Corresponding author. Tel: +86 571 8898 1376; , liuting518@zju.edu.cn, Corresponding author. Tel: +1 713 792 4863; , jchen8@mdanderson.org, Corresponding author. Tel: +86 571 8898 1391; , jhuang@zju.edu.cn organization: Department of Experimental Radiation Oncology, University of Texas M.D. Anderson Cancer Center, TX, Houston, USA – sequence: 8 givenname: Jun surname: Huang fullname: Huang, Jun email: Corresponding author. Tel: +86 571 8898 1376; , liuting518@zju.edu.cn, Corresponding author. Tel: +1 713 792 4863; , jchen8@mdanderson.org, Corresponding author. Tel: +86 571 8898 1391; , jhuang@zju.edu.cn organization: Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, HangzhouZhejiang, China |
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| Keywords | checkpoint initiation RPA checkpoint maintenance DNA damage response homologous recombination repair |
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| Snippet | High expression levels of SLFN11 correlate with the sensitivity of human cancer cells to DNA‐damaging agents. However, little is known about the underlying... High expression levels of SLFN11 correlate with the sensitivity of human cancer cells to DNA-damaging agents. However, little is known about the underlying... High expression levels of SLFN 11 correlate with the sensitivity of human cancer cells to DNA ‐damaging agents. However, little is known about the underlying... |
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| SubjectTerms | Biomarkers Cancer therapies Cell Cycle Checkpoints Cell Line, Tumor checkpoint initiation checkpoint maintenance Deoxyribonucleic acid DNA DNA Damage DNA damage response DNA Replication DNA, Single-Stranded - genetics DNA, Single-Stranded - metabolism EMBO03 EMBO13 Genes, cdc HeLa Cells homologous recombination repair Humans Nuclear Proteins - genetics Nuclear Proteins - metabolism Proteins Recombinational DNA Repair Replication Protein A - genetics Replication Protein A - metabolism RPA |
| Title | SLFN11 inhibits checkpoint maintenance and homologous recombination repair |
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