Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process

Research output: Contribution to journal › Journal article › Research › peer-review

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Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process. / Pfau, Raymond; Tzatsos, Alexandros; Kampranis, Sotirios; Serebrennikova, Oksana B; Bear, Susan E; Tsichlis, Philip N.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 105, No. 6, 12.02.2008, p. 1907-12.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Pfau, R, Tzatsos, A, Kampranis, S, Serebrennikova, OB, Bear, SE & Tsichlis, PN 2008, 'Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process', Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 6, pp. 1907-12. https://doi.org/10.1073/pnas.0711865105

APA

Pfau, R., Tzatsos, A., Kampranis, S., Serebrennikova, O. B., Bear, S. E., & Tsichlis, P. N. (2008). Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process. Proceedings of the National Academy of Sciences of the United States of America, 105(6), 1907-12. https://doi.org/10.1073/pnas.0711865105

Vancouver

Pfau R, Tzatsos A, Kampranis S, Serebrennikova OB, Bear SE, Tsichlis PN. Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process. Proceedings of the National Academy of Sciences of the United States of America. 2008 Feb 12;105(6):1907-12. https://doi.org/10.1073/pnas.0711865105

Author

Pfau, Raymond ; Tzatsos, Alexandros ; Kampranis, Sotirios ; Serebrennikova, Oksana B ; Bear, Susan E ; Tsichlis, Philip N. / Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process. In: Proceedings of the National Academy of Sciences of the United States of America. 2008 ; Vol. 105, No. 6. pp. 1907-12.

Bibtex

@article{7cc20bf1b539446a8e9d9a3ef20517ed,
title = "Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process",
abstract = "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.",
keywords = "Amino Acid Sequence, Animals, Animals, Newborn, Blotting, Northern, Blotting, Western, Cell Transformation, Neoplastic, Cell Transformation, Viral, Embryo, Mammalian, Fibroblasts, Lymphoma, T-Cell, Mice, Molecular Sequence Data, Moloney murine leukemia virus, Oncogene Proteins, Rats, Rats, Inbred F344, Retinoblastoma Protein, Tumor Suppressor Protein p53",
author = "Raymond Pfau and Alexandros Tzatsos and Sotirios Kampranis and Serebrennikova, {Oksana B} and Bear, {Susan E} and Tsichlis, {Philip N}",
year = "2008",
month = feb,
day = "12",
doi = "10.1073/pnas.0711865105",
language = "English",
volume = "105",
pages = "1907--12",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "6",

}

RIS

TY - JOUR

T1 - Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process

AU - Pfau, Raymond

AU - Tzatsos, Alexandros

AU - Kampranis, Sotirios

AU - Serebrennikova, Oksana B

AU - Bear, Susan E

AU - Tsichlis, Philip N

PY - 2008/2/12

Y1 - 2008/2/12

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Animals

KW - Animals, Newborn

KW - Blotting, Northern

KW - Blotting, Western

KW - Cell Transformation, Neoplastic

KW - Cell Transformation, Viral

KW - Embryo, Mammalian

KW - Fibroblasts

KW - Lymphoma, T-Cell

KW - Mice

KW - Molecular Sequence Data

KW - Moloney murine leukemia virus

KW - Oncogene Proteins

KW - Rats

KW - Rats, Inbred F344

KW - Retinoblastoma Protein

KW - Tumor Suppressor Protein p53

U2 - 10.1073/pnas.0711865105

DO - 10.1073/pnas.0711865105

M3 - Journal article

C2 - 18250326

VL - 105

SP - 1907

EP - 1912

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 6

ER -

ID: 159085110