The Corepressor mSin3A Regulates Phosphorylation-Induced Activation, Intranuclear Location, and Stability of AML1

REFERENCES

• Ayer, D. E. 1999. Histone deacetylases: transcriptional repression with SINers and NuRDs. Trends Cell Biol. 9:193–198.
   PubMedGoogle Scholar
• Bruhn, L., Munnerlyn A., and Grosschedl R.. 1997. ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for TCRα enhancer function. Genes Dev. 11:640–653.
   PubMed Web of Science ®Google Scholar
• Chen, L. F., Ito K., Murakami Y., and Ito Y.. 1998. The capacity of polyomavirus enhancer binding protein 2αB (AML1/Cbfa2) to stimulate polyomavirus DNA replication is related to its affinity for the nuclear matrix. Mol. Cell. Biol. 18:4165–4176.
   PubMedGoogle Scholar
• Cowell, I. G. 1994. Repression versus activation in the control of gene transcription. Trends Biochem. Sci. 19:38–42.
   PubMed Web of Science ®Google Scholar
• Golub, T. R., Barker G. F., Bohlander S. K., Hiebert S. W., Ward D. C., Bray-Ward P., Morgan E., Raimondi S. C., Rowley J. D., and Gilliland D. G.. 1995. Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute lymphoblastic leukemia. Proc. Natl. Acad. Sci. USA 92:4917–4921.
   PubMed Web of Science ®Google Scholar
• Herschbach, B. M., and Johnson A. D.. 1993. Transcriptional repression in eukaryotes. Annu. Rev. Cell Biol. 9:479–509.
   PubMedGoogle Scholar
• Huang, G., Shigesada K., Ito K., Wee H. J., Yokomizo T., and Ito Y.. 2001. Dimerization with PEBP2β protects RUNX1/AML1 from ubiquitin-proteasome-mediated degradation. EMBO J. 20:723–733.
   PubMed Web of Science ®Google Scholar
• Imai, Y., Kurokawa M., Izutsu K., Hangaishi A., Maki K., Ogawa S., Chiba S., Mitani K., and Hirai H.. 2001. Mutations of the Smad4 gene in acute myelogeneous leukemia and their functional implications in leukemogenesis. Oncogene 20:88–96.
   PubMed Web of Science ®Google Scholar
• Imai, Y., Kurokawa M., Izutsu K., Hangaishi A., Takeuchi K., Maki K., Ogawa S., Chiba S., Mitani K., and Hirai H.. 2000. Mutations of the AML1 gene in myelodysplastic syndrome and their functional implications in leukemogenesis. Blood 96:3154–3160.
   PubMed Web of Science ®Google Scholar
• Imai, Y., Kurokawa M., Tanaka K., Friedman A. D., Ogawa S., Mitani K., Yazaki Y., and Hirai H.. 1998. TLE, the human homolog of Groucho, interacts with AML1 and acts as a repressor of AML1-induced transactivation. Biochem. Biophys. Res. Commun. 252:582–589.
   PubMed Web of Science ®Google Scholar
• Ishida, N., Kitagawa M., Hatakeyama S., and Nakayama K.. 2000. Phosphorylation at serine 10, a major phosphorylation site of p27(Kip1), increases its protein stability J. Biol. Chem. 275:25146–25154.
   PubMed Web of Science ®Google Scholar
• Kitabayashi, I., Yokoyama A., Shimizu K., and Ohki M.. 1998. Interaction and functional cooperation of the leukemia-associated factors AML1 and p300 in myeloid cell differentiation. EMBO J. 17:2994–3004.
   PubMed Web of Science ®Google Scholar
• Knoepfler, P. S., and Eisenman R. N.. 1999. Sin meets NuRD and other tails of repression. Cell 99:447–450.
   PubMed Web of Science ®Google Scholar
• Koipally, J., Renold A., Kim J., and Georgopoulos K.. 1999. Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes. EMBO J. 18:3090–3100.
   PubMedGoogle Scholar
• Kunkel, T. A., Roberts J. D., and Zakour R. A.. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367–382.
   PubMed Web of Science ®Google Scholar
• Kurokawa, M., Mitani K., Irie K., Matsuyama T., Takahashi T., Chiba S., Yazaki Y., Matsumoto K., and Hirai H.. 1998. The oncoprotein Evi-1 represses TGF-β signalling by inhibiting Smad3. Nature 394:92–96.
   PubMed Web of Science ®Google Scholar
• Kurokawa, M., Tanaka T., Tanaka K., Ogawa S., Mitani K., Yazaki Y., and Hirai H.. 1996. Overexpression of the AML1 proto-oncoprotein in NIH3T3 cells leads to neoplastic transformation depending on the DNA-binding and transactivational potencies. Oncogene 12:883–892.
   PubMed Web of Science ®Google Scholar
• Laherty, C. D., Yang W. M., Sun J. M., Davie J. R., Seto E., and Eisenman R. N.. 1997. Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell 89:349–356.
   PubMed Web of Science ®Google Scholar
• Levanon, D., Goldstein R. E., Bernstein Y., Tang H., Goldenberg D., Stifani S., Paroush Z., and Groner Y.. 1998. Transcriptional repression by AML1 and LEF-1 is mediated by the TLE/Groucho corepressors. Proc. Natl. Acad. Sci. USA 95:11590–11595.
   PubMed Web of Science ®Google Scholar
• Lutterbach, B., and Hiebert S. W.. 2000. Role of the transcription factor AML-1 in acute leukemia and hematopoietic differentiation. Gene 245:223–235.
   PubMed Web of Science ®Google Scholar
• Lutterbach, B., Westendorf J. J., Linggi B., Isaac S., Seto E., and Hiebert S. W.. 2000. A mechanism of repression by acute myeloid leukemia-1, the target of multiple chromosomal translocations in acute leukemia. J. Biol. Chem. 275:651–656.
   PubMed Web of Science ®Google Scholar
• Maciejewski, P. M., Peterson F. C., Anderson P. J., and Brooks C. L.. 1995. Mutation of serine 90 to glutamic acid mimics phosphorylation of bovine prolactin. J. Biol. Chem. 270:27661–27665.
   PubMedGoogle Scholar
• Mitani, K., Ogawa S., Tanaka T., Miyoshi H., Kurokawa M., Mano H., Yazaki Y., Ohki M., and Hirai H.. 1994. Generation of the AML1-EVI-1 fusion gene in the t(3;21)(q26;q22) causes blastic crisis in chronic myelocytic leukemia. EMBO J. 13:504–510.
   PubMed Web of Science ®Google Scholar
• Miyoshi, H., Shimizu K., Kozu T., Maseki N., Kaneko Y., and Ohki M.. 1991. t(8;21) breakpoints on chromosome 21 in acute myeloid leukemia are clustered within a limited region of a single gene, AML1. Proc. Natl. Acad. Sci. USA 88:10431–10434.
   PubMed Web of Science ®Google Scholar
• Murphy, M., Ahn J., Walker K. K., Hoffman W. H., Evans R. M., Levine A. J., and George D. L.. 1999. Transcriptional repression by wild-type p53 utilizes histone deacetylases, mediated by interaction with mSin3A. Genes Dev. 13:2490–2501.
   PubMed Web of Science ®Google Scholar
• Niki, M., Okada H., Takano H., Kuno J., Tani K., Hibino H., Asano S., Ito Y., Satake M., and Noda T.. 1997. Hematopoiesis in the fetal liver is impaired by targeted mutagenesis of a gene encoding a non-DNA binding subunit of the transcription factor, polyomavirus enhancer binding protein 2/core binding factor. Proc. Natl. Acad. Sci. USA 94:5697–5702.
   PubMedGoogle Scholar
• Nuchprayoon, I., Meyers S., Scott L. M., Suzow J., Hiebert S., and Friedman A. D.. 1994. PEBP2/CBF, the murine homolog of the human myeloid AML1 and PEBP2β/CBFβ proto-oncoproteins, regulates the murine myeloperoxidase and neutrophil elastase genes in immature myeloid cells. Mol. Cell. Biol. 14:5558–5568.
   PubMed Web of Science ®Google Scholar
• Ogawa, E., Inuzuka M., Maruyama M., Satake M., Naito-Fujimoto M., Ito Y., and Shigesada K.. 1993. Molecular cloning and characterization of PEBP2β, the heterodimeric partner of a novel Drosophila runt-related DNA binding protein PEBP2α. Virology 194:314–331.
   PubMed Web of Science ®Google Scholar
• Ohki, M. 1993. Molecular basis of the t(8;21) translocation in acute myeloid leukaemia. Semin. Cancer Biol. 4:369–375.
   PubMed Web of Science ®Google Scholar
• Okuda, T., van Deursen J., Hiebert S. W., Grosveld G., and Downing J. R.. 1996. AML1, the target of multiple chromosomal translocations in human leukemia, is essential for normal fetal liver hematopoiesis. Cell 84:321–330.
   PubMed Web of Science ®Google Scholar
• Osato, M., Asou N., Abdalla E., Hoshino K., Yamasaki H., Okubo T., Suzushima H., Takatsuki K., Kanno T., Shigesada K., and Ito Y.. 1999. Biallelic and heterozygous point mutations in the runt domain of the AML1/PEBP2αB gene associated with myeloblastic leukemias. Blood 93:1817–1824.
   PubMed Web of Science ®Google Scholar
• Pazin, M. J., and Kadonaga J. T.. 1997. What's up and down with histone deacetylation and transcription? Cell 89:325–328.
   PubMed Web of Science ®Google Scholar
• Preudhomme, C., Warot-Loze D., Roumier C., Grardel-Duflos N., Garand R., Lai J. L., Dastugue N., Macintyre E., Denis C., Bauters F., Kerckaert J. P., Cosson A., and Fenaux P.. 2000. High incidence of biallelic point mutations in the Runt domain of the AML1/PEBP2αB gene in M0 acute myeloid leukemia and in myeloid malignancies with acquired trisomy 21. Blood 96:2862–2869.
   PubMed Web of Science ®Google Scholar
• Romana, S. P., Mauchauffe M., Le Coniat M., Chumakov I., Le Paslier D., Berger R., and Bernard O. A.. 1995. The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1 gene fusion. Blood 85:3662–3670.
   PubMed Web of Science ®Google Scholar
• Song, W. J., Sullivan M. G., Legare R. D., Hutchings S., Tan X., Kufrin D., Ratajczak J., Resende I. C., Haworth C., Hock R., Loh M., Felix C., Roy D. C., Busque L., Kurnit D., Willman C., Gewirtz A. M., Speck N. A., Bushweller J. H., Li F. P., Gardiner K., Poncz M., Maris J. M., and Gilliland D. G.. 1999. Haploinsufficiency of CBFA2 causes familial thrombocytopenia with propensity to develop acute myelogenous leukaemia. Nat. Genet. 23:166–175.
   PubMed Web of Science ®Google Scholar
• Sun, W., Graves B. J., and Speck N. A.. 1995. Transactivation of the Moloney murine leukemia virus and T-cell receptor β-chain enhancers by cbf and ets requires intact binding sites for both proteins. J. Virol. 69:4941–4949.
   PubMed Web of Science ®Google Scholar
• Takahashi, A., Satake M., Yamaguchi-Iwai Y., Bae S. C., Lu J., Maruyama M., Zhang Y. W., Oka H., Arai N., and Arai K.. 1995. Positive and negative regulation of granulocyte-macrophage colony-stimulating factor promoter activity by AML1-related transcription factor, PEBP2. Blood 86:607–616.
   PubMed Web of Science ®Google Scholar
• Takakura, N., Watanabe T., Suenobu S., Yamada Y., Noda T., Ito Y., Satake M., and Suda T.. 2000. A role for hematopoietic stem cells in promoting angiogenesis. Cell 102:199–209.
   PubMed Web of Science ®Google Scholar
• Tanaka, K., Tanaka T., Kurokawa M., Imai Y., Ogawa S., Mitani K., Yazaki Y., and Hirai H.. 1998. The AML1/ETO(MTG8) and AML1/Evi-1 leukemia-associated chimeric oncoproteins accumulate PEBP2β (CBFβ) in the nucleus more efficiently than wild-type AML1. Blood 91:1688–1699.
   PubMed Web of Science ®Google Scholar
• Tanaka, T., Kurokawa M., Ueki K., Tanaka K., Imai Y., Mitani K., Okazaki K., Sagata N., Yazaki Y., Shibata Y., Kadowaki T., and Hirai H.. 1996. The extracellular signal-regulated kinase pathway phosphorylates AML1, an acute myeloid leukemia gene product, and potentially regulates its transactivation ability. Mol. Cell. Biol. 16:3967–3979.
   PubMed Web of Science ®Google Scholar
• Tanaka, T., Tanaka K., Ogawa S., Kurokawa M., Mitani K., Nishida J., Shibata Y., Yazaki Y., and Hirai H.. 1995. An acute myeloid leukemia gene, AML1, regulates hemopoietic myeloid cell differentiation and transcriptional activation antagonistically by two alternative spliced forms. EMBO J. 14:341–350.
   PubMed Web of Science ®Google Scholar
• Taunton, J., Hassig C. A., and Schreiber S. L.. 1996. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272:408–411.
   PubMed Web of Science ®Google Scholar
• Wood, J. D., Nucifora F. C., Jr., Duan K., Zhang C., Wang J., Kim Y., Schilling G., Sacchi N., Liu J. M., and Ross C. A.. 2000. Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene product, interacts with ETO/MTG8 in the nuclear matrix and represses transcription. J. Cell Biol. 150:939–948.
   PubMedGoogle Scholar
• Yagi, R., Chen L. F., Shigesada K., Murakami Y., and Ito Y.. 1999. A WW domain-containing yes-associated protein (YAP) is a novel transcriptional co-activator. EMBO J. 18:2551–2562.
   PubMed Web of Science ®Google Scholar
• Yang, S. H., Vickers E., Brehm A., Kouzarides T., and Sharrocks A. D.. 2001. Temporal recruitment of the mSin3A-histone deacetylase corepressor complex to the ETS domain transcription factor Elk-1. Mol. Cell. Biol. 21:2802–2814.
   PubMed Web of Science ®Google Scholar
• Zeng, C., McNeil S., Pockwinse S., Nickerson J., Shopland L., Lawrence J. B., Penman S., Hiebert S., Lian J. B., van Wijnen A. J., Stein J. L., and Stein G. S.. 1998. Intranuclear targeting of AML/CBFα regulatory factors to nuclear matrix-associated transcriptional domains. Proc. Natl. Acad. Sci. USA 95:1585–1589.
   PubMed Web of Science ®Google Scholar
• Zeng, C., van Wijnen A. J., Stein J. L., Meyers S., Sun W., Shopland L., Lawrence J. B., Penman S., Lian J. B., Stein G. S., and Hiebert S. W.. 1997. Identification of a nuclear matrix targeting signal in the leukemia and bone-related AML/CBF-α transcription factors. Proc. Natl. Acad. Sci. USA 94:6746–6751.
   PubMed Web of Science ®Google Scholar
• Zhang, D. E., Fujioka K., Hetherington C. J., Shapiro L. H., Chen H. M., Look A. T., and Tenen D. G.. 1994. Identification of a region which directs the monocytic activity of the colony-stimulating factor 1 (macrophage colony-stimulating factor) receptor promoter and binds PEBP2/CBF (AML1). Mol. Cell. Biol. 14:8085–8095.
   PubMed Web of Science ®Google Scholar
• Zilfou, J. T., Hoffman W. H., Sank M., George D. L., and Murphy M.. 2001. The corepressor mSin3A interacts with the proline-rich domain of p53 and protects p53 from proteasome-mediated degradation. Mol. Cell. Biol. 21:3974–3985.
   PubMed Web of Science ®Google Scholar