Cited by 194DNA Repair MechanismsCancer therapeutics and mechanismsPARP inhibition in cancer therapy

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A Small Molecule Targeting Mutagenic Translesion Synthesis Improves Chemotherapy

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Wojtaszek, Jessica L., Chatterjee, Nimrat, Najeeb, Javaria, Ramos, Azucena, Lee, Minhee, Bian, Ke, Xue, Jenny Y., Fenton, Benjamin A., Park, Hyeri, Li, Deyu, Hemann, Michael T., Hong, Jiyong, Walker, Graham C., Zhou, Pei·2019·Cell

DOI 10.1016/j.cell.2019.05.028PMC PMC6644000

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Abstract

Intrinsic and acquired drug resistance and induction of secondary malignancies limit successful chemotherapy. Because mutagenic translesion synthesis (TLS) contributes to chemoresistance as well as treatment-induced mutations, targeting TLS is an attractive avenue for improving chemotherapeutics. However, development of small molecules with high specificity and in vivo efficacy for mutagenic TLS has been challenging. Here, we report the discovery of a small-molecule inhibitor, JH-RE-06, that disrupts mutagenic TLS by preventing recruitment of mutagenic POL ζ. Remarkably, JH-RE-06 targets a nearly featureless surface of REV1 that interacts with the REV7 subunit of POL ζ. Binding of JH-RE-06 induces REV1 dimerization, which blocks the REV1-REV7 interaction and POL ζ recruitment. JH-RE-06 inhibits mutagenic TLS and enhances cisplatin-induced toxicity in cultured human and mouse cell lines. Co-administration of JH-RE-06 with cisplatin suppresses the growth of xenograft human melanomas in mice, establishing a framework for developing TLS inhibitors as a novel class of chemotherapy adjuvants.

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Additional file 6 of USP9X-mediated REV1 deubiquitination promotes lung cancer radioresistance via the action of REV1 as a Rad18 molecular scaffold for cystathionine γ-lyase
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Additional file 2 of USP9X-mediated REV1 deubiquitination promotes lung cancer radioresistance via the action of REV1 as a Rad18 molecular scaffold for cystathionine γ-lyase
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Additional file 4 of USP9X-mediated REV1 deubiquitination promotes lung cancer radioresistance via the action of REV1 as a Rad18 molecular scaffold for cystathionine γ-lyase
Chen, Y., Feng, X., Wu, Z., Yang, Y., Rao, X., Meng, R., Zhang, S., Dong, X., Xu, S., Wu, G., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26726402
Additional file 5 of USP9X-mediated REV1 deubiquitination promotes lung cancer radioresistance via the action of REV1 as a Rad18 molecular scaffold for cystathionine γ-lyase
Chen, Y., Feng, X., Wu, Z., Yang, Y., Rao, X., Meng, R., Zhang, S., Dong, X., Xu, S., Wu, G., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26726405
Additional file 1 of USP9X-mediated REV1 deubiquitination promotes lung cancer radioresistance via the action of REV1 as a Rad18 molecular scaffold for cystathionine γ-lyase
Chen, Y., Feng, X., Wu, Z., Yang, Y., Rao, X., Meng, R., Zhang, S., Dong, X., Xu, S., Wu, G., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25909964
Additional file 3 of USP9X-mediated REV1 deubiquitination promotes lung cancer radioresistance via the action of REV1 as a Rad18 molecular scaffold for cystathionine γ-lyase
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Authors: Wojtaszek, J. L., Chatterjee, N., Najeeb, J., Ramos, A., Lee, M., Bian, K., Xue, J. Y., Fenton, B. A., Park, H., Li, D., Hemann, M. T., Hong, J., Walker, G. C., & Zhou, P.
Affiliations: Duke Medical Center (US)
Massachusetts Institute of Technology (US)
Koch Institute for Integrative Cancer Research At MIT (US)
Duke University (US)
University of Rhode Island (US)
Corresponding author: Hemann, Michael T.
Hong, Jiyong
Walker, Graham C.
Zhou, Pei
ORCID: Wojtaszek, Jessica L.
Chatterjee, Nimrat
Najeeb, Javaria
Lee, Minhee
Bian, Ke
Xue, Jenny Y.
Fenton, Benjamin A.
Park, Hyeri
Li, Deyu
Hemann, Michael T.
Hong, Jiyong
Walker, Graham C.
Zhou, Pei
Venue: Cell
Publisher: Elsevier BV
Published: 2019-06
Volume: 178
Issue: 1
Pages: 152-159.e11
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2019.05.028
PMC: PMC6644000
OpenAlex: W2948035094
Cited by: 194
References: 39
Citations by year: 2026: 22 · 2025: 20 · 2024: 42 · 2023: 23 · 2022: 29 · 2021: 18 · 2020: 32 · 2019: 8
FWCI: 7.19
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 392 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
DSpace@MIT (Massachusetts Institute of Technology) (submittedVersion, cc-by-nc-nd)
OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
Funders: Alexander and Margaret Stewart Trust
Duke University
National Cancer Institute
National Institute of Environmental Health Sciences
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer therapeutics and mechanisms
Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
Keywords: Rev1, REV7, small molecule inhibitors, cisplatin, chemoresistance, melanoma, adjuvant chemotherapy, protein dimerization, drug resistance
MeSH terms: Y-Family DNA Polymerases, Animals, Antineoplastic Agents, Cell Survival, Cisplatin, DNA Damage, DNA-Directed DNA Polymerase, Female, Humans, Mice, Nude, Mice, Transgenic, Neoplasms, Nucleotidyltransferases, Quinolines, Transfection, Mutagenesis, Xenograft Model Antitumor Assays, Cell Line, Tumor, Tumor Burden, Mice, Gene Knockdown Techniques, Mad2 Proteins

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A Small Molecule Targeting Mutagenic Translesion Synthesis Improves Chemotherapy

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