Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process
A common integration site, cloned from MoMuLV-induced rat T cell lymphomas, was mapped immediately upstream of Not dead yet-1 (Ndy1)/KDM2B, a gene expressed primarily in testis, spleen, and thymus, that is also known as FBXL10 or JHDM1B. Ndy1 encodes a nuclear, chromatin-associated protein that harb...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2008-02, Vol.105 (6), p.1907-1912 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Pfau, Raymond Tzatsos, Alexandros Kampranis, Sotirios C Serebrennikova, Oksana B Bear, Susan E Tsichlis, Philip N |
| description | A common integration site, cloned from MoMuLV-induced rat T cell lymphomas, was mapped immediately upstream of Not dead yet-1 (Ndy1)/KDM2B, a gene expressed primarily in testis, spleen, and thymus, that is also known as FBXL10 or JHDM1B. Ndy1 encodes a nuclear, chromatin-associated protein that harbors Jumonji C (JmjC), CXXC, PHD, proline-rich, F-box, and leucine-rich repeat domains. Ndy1 and its homolog Ndy2/KDM2A (FBXL11 or JHDM1A), which is also a target of provirus integration in retrovirus-induced lymphomas, encode proteins that were recently shown to possess Jumonji C-dependent histone H3 K36 dimethyl-demethylase or histone H3 K4 trimethyl-demethylase activities. Here, we show that mouse embryo fibroblasts engineered to express Ndy1 or Ndy2 undergo immortalization in the absence of replicative senescence via a JmjC domain-dependent process that targets the Rb and p53 pathways. Knockdown of endogenous Ndy1 or expression of JmjC domain mutants of Ndy1 promote senescence, suggesting that Ndy1 is a physiological inhibitor of senescence in dividing cells and that inhibition of senescence depends on histone H3 demethylation. |
| doi_str_mv | 10.1073/pnas.0711865105 |
| format | Article |
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Ndy1 encodes a nuclear, chromatin-associated protein that harbors Jumonji C (JmjC), CXXC, PHD, proline-rich, F-box, and leucine-rich repeat domains. Ndy1 and its homolog Ndy2/KDM2A (FBXL11 or JHDM1A), which is also a target of provirus integration in retrovirus-induced lymphomas, encode proteins that were recently shown to possess Jumonji C-dependent histone H3 K36 dimethyl-demethylase or histone H3 K4 trimethyl-demethylase activities. Here, we show that mouse embryo fibroblasts engineered to express Ndy1 or Ndy2 undergo immortalization in the absence of replicative senescence via a JmjC domain-dependent process that targets the Rb and p53 pathways. Knockdown of endogenous Ndy1 or expression of JmjC domain mutants of Ndy1 promote senescence, suggesting that Ndy1 is a physiological inhibitor of senescence in dividing cells and that inhibition of senescence depends on histone H3 demethylation.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0711865105</identifier><identifier>PMID: 18250326</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Amino Acid Sequence ; Animals ; Animals, Newborn ; Antibodies ; Biochemistry ; Biological Sciences ; Blotting, Northern ; Blotting, Western ; Cancer ; Cell cycle ; Cell Transformation, Neoplastic ; Cell Transformation, Viral ; Cellular senescence ; Embryo, Mammalian - chemistry ; Fibroblasts - cytology ; Gene expression ; HCT116 cells ; Histones ; Lymphoma, T-Cell - pathology ; Lymphoma, T-Cell - virology ; Mice ; Molecular Sequence Data ; Moloney murine leukemia virus - physiology ; Oncogene Proteins - physiology ; Oncology ; Proteins ; Proviruses ; Rats ; Rats, Inbred F344 ; Retinoblastoma Protein - metabolism ; Rodents ; Stem cells ; T cell receptors ; T lymphocytes ; Telomeres ; Tumor Suppressor Protein p53 - metabolism ; Tumors</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2008-02, Vol.105 (6), p.1907-1912</ispartof><rights>Copyright 2008 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Feb 12, 2008</rights><rights>2008 by The National Academy of Sciences of the USA</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c616t-49a4b2f379618232e8d3a3432633c6c0b621c41a3a9f0e2659924722654f03d23</citedby><cites>FETCH-LOGICAL-c616t-49a4b2f379618232e8d3a3432633c6c0b621c41a3a9f0e2659924722654f03d23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/105/6.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25451387$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25451387$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18250326$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pfau, Raymond</creatorcontrib><creatorcontrib>Tzatsos, Alexandros</creatorcontrib><creatorcontrib>Kampranis, Sotirios C</creatorcontrib><creatorcontrib>Serebrennikova, Oksana B</creatorcontrib><creatorcontrib>Bear, Susan E</creatorcontrib><creatorcontrib>Tsichlis, Philip N</creatorcontrib><title>Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>A common integration site, cloned from MoMuLV-induced rat T cell lymphomas, was mapped immediately upstream of Not dead yet-1 (Ndy1)/KDM2B, a gene expressed primarily in testis, spleen, and thymus, that is also known as FBXL10 or JHDM1B. Ndy1 encodes a nuclear, chromatin-associated protein that harbors Jumonji C (JmjC), CXXC, PHD, proline-rich, F-box, and leucine-rich repeat domains. Ndy1 and its homolog Ndy2/KDM2A (FBXL11 or JHDM1A), which is also a target of provirus integration in retrovirus-induced lymphomas, encode proteins that were recently shown to possess Jumonji C-dependent histone H3 K36 dimethyl-demethylase or histone H3 K4 trimethyl-demethylase activities. Here, we show that mouse embryo fibroblasts engineered to express Ndy1 or Ndy2 undergo immortalization in the absence of replicative senescence via a JmjC domain-dependent process that targets the Rb and p53 pathways. Knockdown of endogenous Ndy1 or expression of JmjC domain mutants of Ndy1 promote senescence, suggesting that Ndy1 is a physiological inhibitor of senescence in dividing cells and that inhibition of senescence depends on histone H3 demethylation.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Animals, Newborn</subject><subject>Antibodies</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Blotting, Northern</subject><subject>Blotting, Western</subject><subject>Cancer</subject><subject>Cell cycle</subject><subject>Cell Transformation, Neoplastic</subject><subject>Cell Transformation, Viral</subject><subject>Cellular senescence</subject><subject>Embryo, Mammalian - chemistry</subject><subject>Fibroblasts - cytology</subject><subject>Gene expression</subject><subject>HCT116 cells</subject><subject>Histones</subject><subject>Lymphoma, T-Cell - pathology</subject><subject>Lymphoma, T-Cell - virology</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Moloney murine leukemia virus - physiology</subject><subject>Oncogene Proteins - physiology</subject><subject>Oncology</subject><subject>Proteins</subject><subject>Proviruses</subject><subject>Rats</subject><subject>Rats, Inbred F344</subject><subject>Retinoblastoma Protein - metabolism</subject><subject>Rodents</subject><subject>Stem cells</subject><subject>T cell receptors</subject><subject>T lymphocytes</subject><subject>Telomeres</subject><subject>Tumor Suppressor Protein p53 - metabolism</subject><subject>Tumors</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc-P1CAYhhujccfVsye18aCn7n5AoXAxMRN_Zo0H3TOhlI5MWugC3Tie_NOlmcnO6METX8LDk_flK4qnCC4QNORycipeQIMQZxQBvVesEAhUsVrA_WIFgJuK17g-Kx7FuAUAQTk8LM4QxxQIZqvi9xcztibE0velKns12mG3zJ_H7brs_Kisq7R3KZ_WbUrvtJ-CT8a6WNpx9CGpwf4yZbaEnXdWl71tg28HFVMsb63K1lNXZybjOuNSmTXaxPi4eNCrIZonh_O8uH7_7vv6Y3X19cOn9durSjPEUlULVbe4J41gOTzBhndEkTp3IEQzDS3DSNdIESV6MJhRIXDd4DzUPZAOk_Pizd47ze1oOp0jBDXIKdhRhZ30ysq_b5z9ITf-VmJKOKdNFrw6CIK_mU1McrRRm2FQzvg5Spy_NwfiGXz5D7j1c3C5XGYQaaiAJc7lHtLBxxhMf5cEgVxWK5fVyuNq84vnpwWO_GGXJ8Dy8qijkkkkYGnw-r-A7OdhSOZnyuSzPbmNyYc7FNOaIsIX04v9fa-8VJtgo7z-tpQD4FTwBpE_Ps7LTw</recordid><startdate>20080212</startdate><enddate>20080212</enddate><creator>Pfau, Raymond</creator><creator>Tzatsos, Alexandros</creator><creator>Kampranis, Sotirios C</creator><creator>Serebrennikova, Oksana B</creator><creator>Bear, Susan E</creator><creator>Tsichlis, Philip N</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>20080212</creationdate><title>Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process</title><author>Pfau, Raymond ; 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Ndy1 encodes a nuclear, chromatin-associated protein that harbors Jumonji C (JmjC), CXXC, PHD, proline-rich, F-box, and leucine-rich repeat domains. Ndy1 and its homolog Ndy2/KDM2A (FBXL11 or JHDM1A), which is also a target of provirus integration in retrovirus-induced lymphomas, encode proteins that were recently shown to possess Jumonji C-dependent histone H3 K36 dimethyl-demethylase or histone H3 K4 trimethyl-demethylase activities. Here, we show that mouse embryo fibroblasts engineered to express Ndy1 or Ndy2 undergo immortalization in the absence of replicative senescence via a JmjC domain-dependent process that targets the Rb and p53 pathways. Knockdown of endogenous Ndy1 or expression of JmjC domain mutants of Ndy1 promote senescence, suggesting that Ndy1 is a physiological inhibitor of senescence in dividing cells and that inhibition of senescence depends on histone H3 demethylation.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>18250326</pmid><doi>10.1073/pnas.0711865105</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Animals, Newborn Antibodies Biochemistry Biological Sciences Blotting, Northern Blotting, Western Cancer Cell cycle Cell Transformation, Neoplastic Cell Transformation, Viral Cellular senescence Embryo, Mammalian - chemistry Fibroblasts - cytology Gene expression HCT116 cells Histones Lymphoma, T-Cell - pathology Lymphoma, T-Cell - virology Mice Molecular Sequence Data Moloney murine leukemia virus - physiology Oncogene Proteins - physiology Oncology Proteins Proviruses Rats Rats, Inbred F344 Retinoblastoma Protein - metabolism Rodents Stem cells T cell receptors T lymphocytes Telomeres Tumor Suppressor Protein p53 - metabolism Tumors |
| title | Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process |
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