Molecular biology: Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3

Science

Volumn 310, Issue 5746, 2005, Pages 306-310

  Cha, Tai Lung ^a,b,d   Zhou, Binhua P ^a,e   Xia, Weiya ^a   Wu, Yadi ^a   Yang, Cheng Chieh ^a,b   Chen, Chun Te ^a   Ping, Bo ^a   Otte, Arie P ^c   Hung, Mien Chie ^a,b  

^a UNIVERSITY OF TEXAS MD ANDERSON CANCER CENTER   (United States)

^b UNIVERSITY OF TEXAS   (United States)

^c UNIVERSITY OF AMSTERDAM   (Netherlands)

^d NATIONAL DEFENSE UNIVERSITY   (Taiwan)

^e UNIVERSITY OF TEXAS MEDICAL BRANCH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GENES; PHOSPHORS;

METHYLTRANSFERASE ACTIVITY; PHOSPHORYLATION; TRIMETHYLATION; ZESTE HOMOLOGY 2 (EZH2);

MOLECULAR BIOLOGY;

2 MORPHOLINO 8 PHENYLCHROMONE; HISTONE H3; LYSINE; METHYLTRANSFERASE; PROTEIN EZH2; PROTEIN KINASE B; SERINE; UNCLASSIFIED DRUG; 2-(4-MORPHOLINYL)-8-PHENYL-4H-1-BENZOPYRAN-4-ONE; AKT1 PROTEIN, HUMAN; CHROMONE DERIVATIVE; DNA BINDING PROTEIN; ENZYME INHIBITOR; EZH2 PROTEIN, HUMAN; EZH2 PROTEIN, MOUSE; HISTONE; HISTONE LYSINE METHYLTRANSFERASE; HISTONE METHYLTRANSFERASE; HOMEOBOX PROTEIN HOXA9; HOMEODOMAIN PROTEIN; MORPHOLINE DERIVATIVE; ONCOPROTEIN; PROTEIN; PROTEIN SERINE THREONINE KINASE; TRANSCRIPTION FACTOR;

BIOLOGY;

ARTICLE; CARCINOGENESIS; CONTROLLED STUDY; DNA HISTONE INTERACTION; DNA METHYLATION; GENE SILENCING; HUMAN; HUMAN CELL; METHYLATION; NONHUMAN; PRIORITY JOURNAL; PROCESS MODEL; PROTEIN METHYLATION; PROTEIN PHOSPHORYLATION; REGULATORY MECHANISM; REPRESSOR GENE; ANIMAL; CELL LINE; CELL STRAIN 3T3; CELL STRAIN COS1; CELL TRANSFORMATION; CERCOPITHECUS; DRUG ANTAGONISM; GENE EXPRESSION REGULATION; GENETICS; HELA CELL; METABOLISM; MOLECULAR GENETICS; MOUSE; PHOSPHORYLATION; PROTEIN BINDING;

3T3 CELLS; ANIMALS; CELL LINE; CELL TRANSFORMATION, NEOPLASTIC; CERCOPITHECUS AETHIOPS; CHROMONES; COS CELLS; DNA-BINDING PROTEINS; ENZYME INHIBITORS; GENE EXPRESSION REGULATION; HELA CELLS; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HOMEODOMAIN PROTEINS; HUMANS; LYSINE; METHYLATION; MICE; MOLECULAR SEQUENCE DATA; MORPHOLINES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN-SERINE-THREONINE KINASES; PROTEINS; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-AKT; SERINE; TRANSCRIPTION FACTORS;

EID: 26844520965     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1118947     Document Type: Article

References (20)

1. T. Jenuwein, C. D. Allis, Science 293, 1074 (2001).
2. Y. Zhang, D. Reinberg, Genes Dev. 15, 2343 (2001).
3. A. J. Bannister, R. Schneider, T. Kouzarides, Cell 109, 801 (2002).
4. R. J. Sims 3rd, K. Nishioka, D. Reinberg, Trends Genet. 19, 629 (2003).
5. Y. Wang et al., Science 306, 279 (2004).
6. Y. Shi et al., Cell 119, 941 (2004).
7. Y. Zhang, Nature 431, 637 (2004).
8. S. Kubicek, T. Jenuwein, Cell 119, 903 (2004).
9. A. P. Feinberg, B. Tycko, Nat. Rev. Cancer 4, 143 (2004).
10. R. Cao, Y. Zhang, Curr. Opin. Genet. Dev. 14, 155 (2004).
11. A. Kuzmichev, T. Jenuwein, P. Tempst, D. Reinberg, Mol. Cell 14, 183 (2004).
12. F. M. Raaphorst, A. P. Otte, C. J. Meijer, Trends Immunol. 22, 682 (2001).
13. S. Varambally et al., Nature 419, 624 (2002).
14. C. G. Kleer et al., Proc. Natl. Acad. Sci. U.S.A. 100, 11606 (2003).
15. I. Vivanco, C. L. Sawyers, Nat. Rev. Cancer 2, 489 (2002).
16. M. L. Sulis, R. Parsons, Trends Cell Biol. 13, 478 (2003).
17. B. P. Zhou et al., Nat. Cell Biol. 3, 973 (2001).
18. R. Cao, Y. Zhang, Mol. Cell 15, 57 (2004).
19. Materials and Methods and supporting text are available as supporting material on Science Online.
20. This study was supported by the NIH R01 109311 and P01 099031 (to M.-C.H.) and T.-L.C. was partially supported by the Tri-Service General Hospital, Taiwan. We greatly appreciate A. M. Chinnaiyan, D. Reinberg, and Y. Zhang for providing the pCDNA3-Myc-EZH2 plasmid, anti-Eed antibodies, and purified oligonucleosome, respectively. We also thank R. B. Arlinghaus, S. Roth Dent, D. Yu, P. D. McCrea, and M. W. Van Dyke for critically reading this manuscript and J. C. Cheng for editing the manuscript.