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  • 1
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    Myc-induced T cell leukemia in transgenic zebrafish (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-02-08
    Description: The zebrafish is an attractive model organism for studying cancer development because of its genetic accessibility. Here we describe the induction of clonally derived T cell acute lymphoblastic leukemia in transgenic zebrafish expressing mouse c-myc under control of the zebrafish Rag2 promoter. Visualization of leukemic cells expressing a chimeric transgene encoding Myc fused to green fluorescent protein (GFP) revealed that leukemias arose in the thymus, spread locally into gill arches and retro-orbital soft tissue, and then disseminated into skeletal muscle and abdominal organs. Leukemic cells homed back to the thymus in irradiated fish transplanted with GFP-labeled leukemic lymphoblasts. This transgenic model provides a platform for drug screens and for genetic screens aimed at identifying mutations that suppress or enhance c-myc- induced carcinogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Langenau, David M -- Traver, David -- Ferrando, Adolfo A -- Kutok, Jeffery L -- Aster, Jon C -- Kanki, John P -- Lin, Shuo -- Prochownik, Ed -- Trede, Nikolaus S -- Zon, Leonard I -- Look, A Thomas -- CA-06516/CA/NCI NIH HHS/ -- CA-68484/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2003 Feb 7;299(5608):887-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatric Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12574629" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Cell Lineage ; *Cell Transformation, Neoplastic ; Clone Cells ; DNA-Binding Proteins/genetics ; *Disease Models, Animal ; Female ; Fertilization in Vitro ; Gene Expression Profiling ; *Genes, myc ; Green Fluorescent Proteins ; Kidney/pathology ; *Leukemia-Lymphoma, Adult T-Cell/genetics/pathology ; Leukemic Infiltration ; Luminescent Proteins/metabolism ; Male ; Mice ; Mutation ; Neoplasm Transplantation ; Olfactory Bulb/pathology ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/metabolism ; Spleen/pathology ; T-Lymphocytes/immunology/*pathology/physiology ; Thymus Gland/pathology ; Transgenes ; *Zebrafish/embryology/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Contrasting roles of histone 3 lysine 27 demethylases in acute lymphoblastic leukaemia (2014)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2014-08-19
    Description: T-cell acute lymphoblastic leukaemia (T-ALL) is a haematological malignancy with a dismal overall prognosis, including a relapse rate of up to 25%, mainly because of the lack of non-cytotoxic targeted therapy options. Drugs that target the function of key epigenetic factors have been approved in the context of haematopoietic disorders, and mutations that affect chromatin modulators in a variety of leukaemias have recently been identified; however, 'epigenetic' drugs are not currently used for T-ALL treatment. Recently, we described that the polycomb repressive complex 2 (PRC2) has a tumour-suppressor role in T-ALL. Here we delineated the role of the histone 3 lysine 27 (H3K27) demethylases JMJD3 and UTX in T-ALL. We show that JMJD3 is essential for the initiation and maintenance of T-ALL, as it controls important oncogenic gene targets by modulating H3K27 methylation. By contrast, we found that UTX functions as a tumour suppressor and is frequently genetically inactivated in T-ALL. Moreover, we demonstrated that the small molecule inhibitor GSKJ4 (ref. 5) affects T-ALL growth, by targeting JMJD3 activity. These findings show that two proteins with a similar enzymatic function can have opposing roles in the context of the same disease, paving the way for treating haematopoietic malignancies with a new category of epigenetic inhibitors.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4209203/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4209203/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ntziachristos, Panagiotis -- Tsirigos, Aristotelis -- Welstead, G Grant -- Trimarchi, Thomas -- Bakogianni, Sofia -- Xu, Luyao -- Loizou, Evangelia -- Holmfeldt, Linda -- Strikoudis, Alexandros -- King, Bryan -- Mullenders, Jasper -- Becksfort, Jared -- Nedjic, Jelena -- Paietta, Elisabeth -- Tallman, Martin S -- Rowe, Jacob M -- Tonon, Giovanni -- Satoh, Takashi -- Kruidenier, Laurens -- Prinjha, Rab -- Akira, Shizuo -- Van Vlierberghe, Pieter -- Ferrando, Adolfo A -- Jaenisch, Rudolf -- Mullighan, Charles G -- Aifantis, Iannis -- 1R01CA105129/CA/NCI NIH HHS/ -- 1R01CA133379/CA/NCI NIH HHS/ -- 1R01CA149655/CA/NCI NIH HHS/ -- 5 T32 CA009161-37/CA/NCI NIH HHS/ -- 5P30CA16087-31/CA/NCI NIH HHS/ -- 5R01CA169784/CA/NCI NIH HHS/ -- 5R01CA173636/CA/NCI NIH HHS/ -- K99 CA188293/CA/NCI NIH HHS/ -- K99CA188293/CA/NCI NIH HHS/ -- P30 CA014051/CA/NCI NIH HHS/ -- P30 CA016087/CA/NCI NIH HHS/ -- P30 CA016087-30/CA/NCI NIH HHS/ -- P30 CA021765/CA/NCI NIH HHS/ -- R01 CA105129/CA/NCI NIH HHS/ -- R01 CA133379/CA/NCI NIH HHS/ -- R01 CA149655/CA/NCI NIH HHS/ -- R01 CA173636/CA/NCI NIH HHS/ -- R01CA120196/CA/NCI NIH HHS/ -- R37 HD045022/HD/NICHD NIH HHS/ -- R37-HD04502/HD/NICHD NIH HHS/ -- U10 CA180820/CA/NCI NIH HHS/ -- U10 CA180827/CA/NCI NIH HHS/ -- U10 CA21115/CA/NCI NIH HHS/ -- U24 CA114737/CA/NCI NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2014 Oct 23;514(7523):513-7. doi: 10.1038/nature13605. Epub 2014 Aug 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Howard Hughes Medical Institute and Department of Pathology, NYU School of Medicine, New York, New York 10016, USA [2] NYU Cancer Institute and Helen L. and Martin S. Kimmel Center for Stem Cell Biology, NYU School of Medicine, New York, New York 10016, USA [3]. ; 1] Howard Hughes Medical Institute and Department of Pathology, NYU School of Medicine, New York, New York 10016, USA [2] Center for Health Informatics and Bioinformatics, NYU School of Medicine, New York, New York 10016, USA [3]. ; 1] Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142, USA [2] Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA [3]. ; 1] Howard Hughes Medical Institute and Department of Pathology, NYU School of Medicine, New York, New York 10016, USA [2] NYU Cancer Institute and Helen L. and Martin S. Kimmel Center for Stem Cell Biology, NYU School of Medicine, New York, New York 10016, USA. ; Institute for Cancer Genetics, Columbia University Medical Center, New York, New York 10032, USA. ; Department of Pathology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA. ; Department of Computational Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA. ; Montefiore Medical Center North, Bronx, New York, New York 10467, USA. ; Memorial Sloan Kettering Cancer Center, New York, New York 10065, USA. ; 1] Technion, Israel Institute of Technology, Haifa 31096, Israel [2] Shaare Zedek Medical Center, Jerusalem 9103102, Israel. ; Functional Genomics of Cancer Unit, Division of Molecular Oncology, Istituto di Ricovero e Cura a Carattere Scientifico (IRCCS) San Raffaele Scientific Institute, 20132 Milan, Italy. ; 1] Laboratory of Host Defense, WPI Immunology Frontier Research Center (WPI IFReC), Osaka University, 3-1 Yamada-oka, Suita, Osaka 565-0871, Japan [2] Department of Host Defense, Research Institute for Microbial Diseases (RIMD), Osaka University, 3-1Yamada-oka, Suita, Osaka 565-0871, Japan. ; Epinova DPU, Immuno-Inflammation Therapy Area, GlaxoSmithKline R&D, Medicines Research Centre, GunnelsWood Road, Stevenage SG1 2NY, UK. ; 1] Institute for Cancer Genetics, Columbia University Medical Center, New York, New York 10032, USA [2] Center for Medical Genetics, Ghent University Hospital, 9000 Ghent, Belgium. ; 1] Institute for Cancer Genetics, Columbia University Medical Center, New York, New York 10032, USA [2] Department of Pathology, Columbia University Medical Center, New York, New York 10032, USA [3] Department of Pediatrics, Columbia University Medical Center, New York, New York 10032, USA. ; 1] Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142, USA [2] Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25132549" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Benzazepines/pharmacology ; Epigenesis, Genetic/drug effects ; Histone Demethylases/genetics/*metabolism ; Histones/chemistry/metabolism ; Jumonji Domain-Containing Histone Demethylases/antagonists & ; inhibitors/*metabolism ; Lysine/metabolism ; Methylation/drug effects ; Mice ; Precursor Cell Lymphoblastic Leukemia-Lymphoma/drug ; therapy/*enzymology/genetics/pathology ; Pyrimidines/pharmacology ; Tumor Suppressor Proteins/genetics/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-12-22
    Description: MCL1 is essential for the survival of stem and progenitor cells of multiple lineages, and is unique among pro-survival BCL2 family members in that it is rapidly turned over through the action of ubiquitin ligases. B- and mantle-cell lymphomas, chronic myeloid leukaemia, and multiple myeloma, however, express abnormally high levels of MCL1, contributing to chemoresistance and disease relapse. The mechanism of MCL1 overexpression in cancer is not well understood. Here we show that the deubiquitinase USP9X stabilizes MCL1 and thereby promotes cell survival. USP9X binds MCL1 and removes the Lys 48-linked polyubiquitin chains that normally mark MCL1 for proteasomal degradation. Increased USP9X expression correlates with increased MCL1 protein in human follicular lymphomas and diffuse large B-cell lymphomas. Moreover, patients with multiple myeloma overexpressing USP9X have a poor prognosis. Knockdown of USP9X increases MCL1 polyubiquitination, which enhances MCL1 turnover and cell killing by the BH3 mimetic ABT-737. These results identify USP9X as a prognostic and therapeutic target, and they show that deubiquitinases may stabilize labile oncoproteins in human malignancies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwickart, Martin -- Huang, Xiaodong -- Lill, Jennie R -- Liu, Jinfeng -- Ferrando, Ronald -- French, Dorothy M -- Maecker, Heather -- O'Rourke, Karen -- Bazan, Fernando -- Eastham-Anderson, Jeffrey -- Yue, Peng -- Dornan, David -- Huang, David C S -- Dixit, Vishva M -- England -- Nature. 2010 Jan 7;463(7277):103-7. doi: 10.1038/nature08646. Epub 2009 Dec 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiological Chemistry, Genentech, Inc., 1 DNA Way, South San Francisco, California 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20023629" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis/drug effects ; Biphenyl Compounds/pharmacology ; Cell Line ; Cell Line, Tumor ; Cell Survival ; DNA Damage ; Etoposide/pharmacology ; Female ; Gene Expression Regulation, Neoplastic ; Gene Knockdown Techniques ; Half-Life ; Humans ; Lysine/metabolism ; Mice ; Mice, SCID ; Myeloid Cell Leukemia Sequence 1 Protein ; Neoplasms/diagnosis/*metabolism/*pathology ; Nitrophenols/pharmacology ; Phosphorylation/radiation effects ; Piperazines/pharmacology ; Polyubiquitin/*metabolism ; Prognosis ; Protein Binding/radiation effects ; Protein Stability ; Proto-Oncogene Proteins c-bcl-2/genetics/*metabolism ; RNA Interference ; Sulfonamides/pharmacology ; Taxoids/pharmacology ; Ubiquitin Thiolesterase/deficiency/genetics/*metabolism ; Ubiquitination ; Ultraviolet Rays ; Xenograft Model Antitumor Assays
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 4
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    COP1 is a tumour suppressor that causes degradation of ETS transcription factors (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-05-17
    Description: The proto-oncogenes ETV1, ETV4 and ETV5 encode transcription factors in the E26 transformation-specific (ETS) family, which includes the most frequently rearranged and overexpressed genes in prostate cancer. Despite being critical regulators of development, little is known about their post-translational regulation. Here we identify the ubiquitin ligase COP1 (also known as RFWD2) as a tumour suppressor that negatively regulates ETV1, ETV4 and ETV5. ETV1, which is mutated in prostate cancer more often, was degraded after being ubiquitinated by COP1. Truncated ETV1 encoded by prostate cancer translocation TMPRSS2:ETV1 lacks the critical COP1 binding motifs and was 50-fold more stable than wild-type ETV1. Almost all patient translocations render ETV1 insensitive to COP1, implying that this confers a selective advantage to prostate epithelial cells. Indeed, COP1 deficiency in mouse prostate elevated ETV1 and produced increased cell proliferation, hyperplasia, and early prostate intraepithelial neoplasia. Combined loss of COP1 and PTEN enhanced the invasiveness of mouse prostate adenocarcinomas. Finally, rare human prostate cancer samples showed hemizygous loss of the COP1 gene, loss of COP1 protein, and elevated ETV1 protein while lacking a translocation event. These findings identify COP1 as a tumour suppressor whose downregulation promotes prostatic epithelial cell proliferation and tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vitari, Alberto C -- Leong, Kevin G -- Newton, Kim -- Yee, Cindy -- O'Rourke, Karen -- Liu, Jinfeng -- Phu, Lilian -- Vij, Rajesh -- Ferrando, Ronald -- Couto, Suzana S -- Mohan, Sankar -- Pandita, Ajay -- Hongo, Jo-Anne -- Arnott, David -- Wertz, Ingrid E -- Gao, Wei-Qiang -- French, Dorothy M -- Dixit, Vishva M -- England -- Nature. 2011 May 15;474(7351):403-6. doi: 10.1038/nature10005.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiological Chemistry, Genentech, Inc., 1 DNA Way, South San Francisco, California 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21572435" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Carrier Proteins/metabolism ; Cell Line ; Cell Line, Tumor ; Cell Proliferation ; Cell Transformation, Neoplastic ; DNA-Binding Proteins/genetics/metabolism ; Humans ; Male ; Mice ; Nuclear Proteins/deficiency/*metabolism ; PTEN Phosphohydrolase/deficiency ; Prostatic Neoplasms/metabolism/pathology ; Protein Binding ; Proto-Oncogene Proteins c-ets/*metabolism ; Transcription Factors/genetics/metabolism ; Tumor Suppressor Proteins/*metabolism ; Ubiquitin-Protein Ligases/deficiency/genetics/*metabolism ; Ubiquitination
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 5
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    Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-02-22
    Description: Receptor-interacting protein kinase 1 (RIPK1) and RIPK3 trigger pro-inflammatory cell death termed "necroptosis." Studies with RIPK3-deficient mice or the RIPK1 inhibitor necrostatin-1 suggest that necroptosis exacerbates pathology in many disease models. We engineered mice expressing catalytically inactive RIPK3 D161N or RIPK1 D138N to determine the need for the active kinase in the whole animal. Unexpectedly, RIPK3 D161N promoted lethal RIPK1- and caspase-8-dependent apoptosis. In contrast, mice expressing RIPK1 D138N were viable and, like RIPK3-deficient mice, resistant to tumor necrosis factor (TNF)-induced hypothermia. Cells expressing RIPK1 D138N were resistant to TNF-induced necroptosis, whereas TNF-induced signaling pathways promoting gene transcription were unperturbed. Our data indicate that the kinase activity of RIPK3 is essential for necroptosis but also governs whether a cell activates caspase-8 and dies by apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newton, Kim -- Dugger, Debra L -- Wickliffe, Katherine E -- Kapoor, Neeraj -- de Almagro, M Cristina -- Vucic, Domagoj -- Komuves, Laszlo -- Ferrando, Ronald E -- French, Dorothy M -- Webster, Joshua -- Roose-Girma, Merone -- Warming, Soren -- Dixit, Vishva M -- New York, N.Y. -- Science. 2014 Mar 21;343(6177):1357-60. doi: 10.1126/science.1249361. Epub 2014 Feb 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiological Chemistry, Genentech, 1 DNA Way, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24557836" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Caspase 8/genetics/metabolism ; Cell Survival ; Embryo Loss ; Embryonic Development ; Enteritis/pathology ; Fas-Associated Death Domain Protein/metabolism ; Gene Knock-In Techniques ; Intestine, Large/pathology ; Intestine, Small/pathology ; Mice ; *Necrosis ; Receptor-Interacting Protein Serine-Threonine Kinases/antagonists & ; inhibitors/genetics/*metabolism ; Tumor Necrosis Factor-alpha/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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