Inhibiting WEE1 Selectively Kills Histone H3K36me3-Deficient Cancers by dNTP Starvation

Histone H3K36 trimethylation (H3K36me3) is frequently lost in multiple cancer types, identifying it as an important therapeutic target. Here we identify a synthetic lethal interaction in which H3K36me3-deficient cancers are acutely sensitive to WEE1 inhibition. We show that RRM2, a ribonucleotide re...

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Published in:Cancer cell Vol. 28; no. 5; pp. 557 - 568
Main Authors: Pfister, Sophia X, Markkanen, Enni, Jiang, Yanyan, Sarkar, Sovan, Woodcock, Mick, Orlando, Giulia, Mavrommati, Ioanna, Pai, Chen-Chun, Zalmas, Lykourgos-Panagiotis, Drobnitzky, Neele, Dianov, Grigory L, Verrill, Clare, Macaulay, Valentine M, Ying, Songmin, La Thangue, Nicholas B, D'Angiolella, Vincenzo, Ryan, Anderson J, Humphrey, Timothy C
Format: Journal Article
Language:English
Published: United States 09.11.2015
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ISSN:1878-3686
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Abstract Histone H3K36 trimethylation (H3K36me3) is frequently lost in multiple cancer types, identifying it as an important therapeutic target. Here we identify a synthetic lethal interaction in which H3K36me3-deficient cancers are acutely sensitive to WEE1 inhibition. We show that RRM2, a ribonucleotide reductase subunit, is the target of this synthetic lethal interaction. RRM2 is regulated by two pathways here: first, H3K36me3 facilitates RRM2 expression through transcription initiation factor recruitment; second, WEE1 inhibition degrades RRM2 through untimely CDK activation. Therefore, WEE1 inhibition in H3K36me3-deficient cells results in RRM2 reduction, critical dNTP depletion, S-phase arrest, and apoptosis. Accordingly, this synthetic lethality is suppressed by increasing RRM2 expression or inhibiting RRM2 degradation. Finally, we demonstrate that WEE1 inhibitor AZD1775 regresses H3K36me3-deficient tumor xenografts.
AbstractList Histone H3K36 trimethylation (H3K36me3) is frequently lost in multiple cancer types, identifying it as an important therapeutic target. Here we identify a synthetic lethal interaction in which H3K36me3-deficient cancers are acutely sensitive to WEE1 inhibition. We show that RRM2, a ribonucleotide reductase subunit, is the target of this synthetic lethal interaction. RRM2 is regulated by two pathways here: first, H3K36me3 facilitates RRM2 expression through transcription initiation factor recruitment; second, WEE1 inhibition degrades RRM2 through untimely CDK activation. Therefore, WEE1 inhibition in H3K36me3-deficient cells results in RRM2 reduction, critical dNTP depletion, S-phase arrest, and apoptosis. Accordingly, this synthetic lethality is suppressed by increasing RRM2 expression or inhibiting RRM2 degradation. Finally, we demonstrate that WEE1 inhibitor AZD1775 regresses H3K36me3-deficient tumor xenografts.
Author Sarkar, Sovan
D'Angiolella, Vincenzo
Pai, Chen-Chun
Ryan, Anderson J
Verrill, Clare
Jiang, Yanyan
Mavrommati, Ioanna
Ying, Songmin
Humphrey, Timothy C
Woodcock, Mick
Orlando, Giulia
Pfister, Sophia X
La Thangue, Nicholas B
Dianov, Grigory L
Drobnitzky, Neele
Macaulay, Valentine M
Markkanen, Enni
Zalmas, Lykourgos-Panagiotis
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  surname: Pfister
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  organization: CRUK MRC Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford, Oxford OX3 7DQ, UK
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  surname: Markkanen
  fullname: Markkanen, Enni
  organization: CRUK MRC Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford, Oxford OX3 7DQ, UK; Institute of Pharmacology and Toxicology, Vetsuisse Faculty, Winterthurerstrasse 260, 8057 Zürich, Switzerland
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  givenname: Yanyan
  surname: Jiang
  fullname: Jiang, Yanyan
  organization: CRUK MRC Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford, Oxford OX3 7DQ, UK
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  organization: CRUK MRC Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford, Oxford OX3 7DQ, UK
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  givenname: Chen-Chun
  surname: Pai
  fullname: Pai, Chen-Chun
  organization: CRUK MRC Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford, Oxford OX3 7DQ, UK
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  surname: Zalmas
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  organization: Department of Oncology, University of Oxford, Old Road Campus Research Building, Oxford OX3 7DQ, UK
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  givenname: Neele
  surname: Drobnitzky
  fullname: Drobnitzky, Neele
  organization: CRUK MRC Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford, Oxford OX3 7DQ, UK
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  givenname: Grigory L
  surname: Dianov
  fullname: Dianov, Grigory L
  organization: CRUK MRC Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford, Oxford OX3 7DQ, UK; Institute of Cytology and Genetics RAS, Novosibirsk 630090, Russia
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  givenname: Clare
  surname: Verrill
  fullname: Verrill, Clare
  organization: Department of Cellular Pathology, Oxford University Hospitals NHS Trust, John Radcliffe Hospital, Oxford OX3 9DU, UK
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  givenname: Valentine M
  surname: Macaulay
  fullname: Macaulay, Valentine M
  organization: Department of Oncology, University of Oxford, Old Road Campus Research Building, Oxford OX3 7DQ, UK; Oxford Cancer and Haematology Centre, Oxford University Hospitals NHS Trust, Churchill Hospital, Oxford OX3 7LJ, UK
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  givenname: Songmin
  surname: Ying
  fullname: Ying, Songmin
  organization: Department of Respiratory and Critical Care Medicine of the Second Affiliated Hospital and Department of Pharmacology, Zhejiang University School of Medicine, Hangzhou 310058, China
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  surname: La Thangue
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  email: timothy.humphrey@oncology.ox.ac.uk
  organization: CRUK MRC Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford, Oxford OX3 7DQ, UK. Electronic address: timothy.humphrey@oncology.ox.ac.uk
BackLink https://www.ncbi.nlm.nih.gov/pubmed/26602815$$D View this record in MEDLINE/PubMed
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PMID 26602815
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PublicationTitle Cancer cell
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PublicationYear 2015
References 26555168 - Cancer Cell. 2015 Nov 9;28(5):545-547. doi: 10.1016/j.ccell.2015.10.009.
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Snippet Histone H3K36 trimethylation (H3K36me3) is frequently lost in multiple cancer types, identifying it as an important therapeutic target. Here we identify a...
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SubjectTerms Amino Acid Sequence
Animals
Base Sequence
Blotting, Western
Cell Cycle Proteins - antagonists & inhibitors
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Cell Line, Tumor
Cell Survival - drug effects
Cell Survival - genetics
Gene Expression Regulation, Neoplastic - drug effects
Histone-Lysine N-Methyltransferase - genetics
Histone-Lysine N-Methyltransferase - metabolism
Histones - genetics
Histones - metabolism
Humans
Lysine - genetics
Lysine - metabolism
Methylation - drug effects
Mice, Inbred BALB C
Mice, Nude
Molecular Sequence Data
Neoplasms - genetics
Neoplasms - metabolism
Neoplasms - prevention & control
Nuclear Proteins - antagonists & inhibitors
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Nucleotides - genetics
Nucleotides - metabolism
Protein-Tyrosine Kinases - antagonists & inhibitors
Protein-Tyrosine Kinases - genetics
Protein-Tyrosine Kinases - metabolism
Pyrazoles - pharmacology
Pyrimidines - pharmacology
Pyrimidinones
Reverse Transcriptase Polymerase Chain Reaction
Ribonucleoside Diphosphate Reductase - genetics
Ribonucleoside Diphosphate Reductase - metabolism
RNA Interference
Sequence Homology, Amino Acid
Sequence Homology, Nucleic Acid
Xenograft Model Antitumor Assays
Title Inhibiting WEE1 Selectively Kills Histone H3K36me3-Deficient Cancers by dNTP Starvation
URI https://www.ncbi.nlm.nih.gov/pubmed/26602815
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