Jmjd2c histone demethylase enhances the expression of Mdm2 oncogene

Biochemical and Biophysical Research Communications

Volumn 389, Issue 2, 2009, Pages 366-371

  Ishimura, Akihiko ^a   Terashima, Minoru ^a   Kimura, Hiroshi ^b   Akagi, Keiko ^c   Suzuki, Yutaka ^d   Sugano, Sumio ^d   Suzuki, Takeshi ^a  

^a KANAZAWA UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c OHIO STATE UNIVERSITY   (United States)

^d UNIVERSITY OF TOKYO   (Japan)

Author keywords

Histone demethylase; JmjC domain; Oncogene; p53; Transcription

Indexed keywords

HISTONE DEMETHYLASE; HISTONE H3; ISOENZYME; PROTEIN MDM2; PROTEIN P53; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CARCINOGENESIS; CONTROLLED STUDY; DEMETHYLATION; ENZYME ACTIVITY; GENE EXPRESSION REGULATION; GENE OVEREXPRESSION; GENE TARGETING; GENETIC TRANSCRIPTION; JMJD2C ONCOGENE; MOUSE; NONHUMAN; ONCOGENE; PRIORITY JOURNAL; PROMOTER REGION; TUMOR SUPPRESSOR GENE;

ANIMALS; CELL LINE; CELL TRANSFORMATION, NEOPLASTIC; CHROMATIN IMMUNOPRECIPITATION; GENE EXPRESSION REGULATION, NEOPLASTIC; GENE KNOCKDOWN TECHNIQUES; HISTONE DEACETYLASES; HISTONES; METHYLATION; MICE; OXIDOREDUCTASES, N-DEMETHYLATING; PROMOTER REGIONS, GENETIC; PROTO-ONCOGENE PROTEINS C-MDM2;

EID: 70349327373     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.08.155     Document Type: Article

References (23)

1. Kouzarides T. Chromatin modifications and their function. Cell 128 (2007) 693-705
2. Klose R.J., Kallin E.M., and Zhang Y. JmjC-domain-containing proteins and histone demethylation. Nat. Rev. Genet. 7 (2006) 715-727
3. Shi Y. Histone lysine demethylases: emerging roles in development, physiology and disease. Nat. Rev. Genet. 8 (2007) 829-833
4. Cloos P.A., Christensen J., Agger K., and Helin K. Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. Genes Dev. 22 (2008) 1115-1140
5. Bernstein B.E., Kamal M., Lindblad-Toh K., Bekiranov S., Bailey D.K., Huebert D.J., McMahon S., Karlsson E.K., Kulbokas III E.J., Gingeras T.R., Schreiber S.L., and Lander E.S. Genomic maps and comparative analysis of histone modifications in human and mouse. Cell 120 (2005) 169-181
6. Barski A., Cuddapah S., Cui K., Roh T.Y., Schones D.E., Wang Z., Wei G., Chepelev I., and Zhao K. High-resolution profiling of histone methylations in the human genome. Cell 129 (2007) 823-837
7. Suzuki T., Shen H., Akagi K., Morse H.C., Malley J.D., Naiman D.Q., Jenkins N.A., and Copeland N.G. New genes involved in cancer identified by retroviral tagging. Nat. Genet. 32 (2002) 166-174
8. Suzuki T., Minehata K., Akagi K., Jenkins N.A., and Copeland N.G. Tumor suppressor gene identification using retroviral insertional mutagenesis in Blm-deficient mice. EMBO J. 25 (2006) 3422-3431
9. Cloos P.A., Christensen J., Agger K., Maiolica A., Rappsilber J., Antal T., Hansen K.H., and Helin K. The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3. Nature 442 (2006) 307-311
10. Whetstine J.R., Nottke A., Lan F., Huarte M., Smolikov S., Chen Z., Spooner E., Li E., Zhang G., Colaiacovo M., and Shi Y. Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. Cell 125 (2006) 467-481
11. Yang Z.Q., Imoto I., Fukuda Y., Pimkhaokham A., Shimada Y., Imamura M., Sugano S., Nakamura Y., and Inazawa J. Identification of a novel gene, GASC1, within an amplicon at 9p23-24 frequently detected in esophageal cancer cell lines. Cancer Res. 60 (2000) 4735-4739
12. Wissmann M., Yin N., Muller J.M., Greschik H., Fodor B.D., Jenuwein T., Vogler C., Schneider R., Gunther T., Buettner R., Metzger E., and Schule R. Cooperative demethylation by JMJD2C and LSD1 promotes androgen receptor-dependent gene expression. Nat. Cell Biol. 9 (2007) 347-353
13. Kimura H., Hayashi-Takanaka Y., Goto Y., Takizawa N., and Nozaki N. The organization of histone H3 modifications as revealed by a panel of specific monoclonal antibodies. Cell Struct. Funct. 33 (2008) 61-73
14. Tsuchihara K., Suzuki Y., Wakaguri H., Irie T., Tanimoto K., Hashimoto S., Matsushima K., Mizushima-Sugano J., Yamashita R., Nakai K., Bentley D., Esumi H., and Sugano S. Massive transcriptional start site analysis of human genes in hypoxia cells. Nucleic Acids Res. 37 (2009) 2249-2263
15. Onel K., and Cordon-Cardo C. MDM2 and prognosis. Mol. Cancer Res. 2 (2004) 1-8
16. Barak Y., Gottlieb E., Juven-Gershon T., and Oren M. Regulation of mdm2 expression by p53: alternative promoters produce transcripts with nonidentical translation potential. Genes Dev. 8 (1994) 1739-1749
17. Kruse J.P., and Gu W. Modes of p53 regulation. Cell 137 (2009) 609-622
18. Klose R.J., Yamane K., Bae Y., Zhang D., Erdjument-Bromage H., Tempst P., Wong J., and Zhang Y. The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36. Nature 442 (2006) 312-316
19. Loh Y.H., Zhang W., Chen X., George J., and Ng H.H. Jmjd1a and Jmjd2c histone H3 Lys 9 demethylases regulate self-renewal in embryonic stem cells. Genes Dev. 21 (2007) 2545-2557
20. Agger K., Cloos P.A., Christensen J., Pasini D., Rose S., Rappsilber J., Issaeva I., Canaani E., Salcini A.E., and Helin K. UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development. Nature 449 (2007) 731-734
21. Vinatzer U., Gollinger M., Mullauer L., Raderer M., Chott A., and Streubel B. Mucosa-associated lymphoid tissue lymphoma: novel translocations including rearrangements of ODZ2, JMJD2C, and CNN3. Clin. Cancer Res. 14 (2008) 6426-6431
22. Peters A.H., O'Carroll D., Scherthan H., Mechtler K., Sauer S., Schofer C., Weipoltshammer K., Pagani M., Lachner M., Kohlmaier A., Opravil S., Doyle M., Sibilia M., and Jenuwein T. Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability. Cell 107 (2001) 323-337
23. Ganguli G., and Wasylyk B. P53-independent functions of MDM2. Mol. Cancer Res. 1 (2003) 1027-1035