The extracellular signal-regulated kinase pathway phosphorylates AML1, an acute myeloid leukemia gene product, and potentially regulates its transactivation ability

Molecular and Cellular Biology

Volumn 16, Issue 7, 1996, Pages 3967-3979

  Tanaka, Tomoyuki ^a,c   Kurokawa, Mineo ^a   Ueki, Kohjiro ^a   Tanaka, Kozo ^a   Imai, Yoichi ^a   Mitani, Kinuko ^a   Okazaki, Kenji ^b,d   Sagata, Noriyuki ^b,e   Yazaki, Yoshio ^a   Shibata, Yoichi ^a   Kadowaki, Takashi ^a   Hirai, Hisamaru ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b KURUME UNIVERSITY   (Japan)

^c RESEARCH INSTITUTE OF MOLECULAR PATHOLOGY   (Austria)

^d BIOMOL ENG RESEARCH INSTITUTE   (Japan)

^e KYUSHU UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; INTERLEUKIN 3; MITOGEN ACTIVATED PROTEIN KINASE;

ACUTE GRANULOCYTIC LEUKEMIA; ANIMAL CELL; ARTICLE; COLONY FORMATION; CONTROLLED STUDY; HEMATOPOIESIS; HEMATOPOIETIC CELL; HUMAN; LEUKEMOGENESIS; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN PHOSPHORYLATION; RAT; REGULATORY MECHANISM; SIGNAL TRANSDUCTION; TRANSACTIVATION;

EID: 8944230662     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.7.3967     Document Type: Article

References (102)

1. Adams, P. D., and P. J. Parker. 1992. Activation of mitogen-activated protein (MAP) kinase by a MAP kinase-kinase. J. Biol. Chem. 267:13135-13137.
2. Alberola, I. J., K. A. Forbush, R. Seger, E. G. Krebs, and R. M. Perlmutter. 1995. Selective requirement for MAP kinase activation in thymocyte differentiation. Nature (London) 373:620-623.
3. Alessandrini, A., C. M. Crews, and R. L. Erikson. 1992. Phorbol ester stimulates a protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product. Proc. Natl. Acad. Sci. USA 89:8200-8204.
4. Bae, S. C., E. Ogawa, M. Maruyama, H. Oka, M. Satake, K. Shigesada, N. A. Jenkins, D. J. Gilbert, N. G. Copeland, and Y. Ito. 1994. PEBP2αB/mouse AML1 consists of multiple isoforms that possess differential transactivation potentials. Mol. Cell. Biol. 14:3242-3452.
5. Bae, S. C., E. Takahashi, Y. W. Zhang, E. Ogawa, K. Shigesada, Y. Numbs, M. Sataka, and Y. Ito. 1995, Cloning, mapping and expression of PEBP2αC, a third gene encoding the mammalian Runt domain. Gene 159:245-248.
6. Bae, S. C., I. Y. Yamaguchi, E. Ogawa, M. Maruyama, M. Inuzuka, H. Kagoshima, K. Shigesada, M. Satake, and Y. Ito. 1993. Isolation of PEBP2αB cDNA representing the mouse homolog of human acute myeloid leukemia gene, AML1. Oncogene 8:809-814.
7. Bernstein, L. R., D. K. Ferris, N. H. Colburn, and M. E. Sobel. 1994. A family of mitogen-activated protein kinase-related proteins interacts in vivo with activator protein-1 transcription factor. J. Biol. Chem. 269:9401-9404.
8. Boyle, W. J., P. van der Geer, and T. Hunter. 1991. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201:110-149.
9. Chen, L. F., K. Ito, Y. Murakami, and Y. Ito. 1995. Stimulation of polyomavirus DNA replication by a transcription factor PEBP2, abstr. 441, p. 161. In Abstracts of the 54th Annual Meeting of the Japanese Cancer Association 1995. Japanese Cancer Association, Tokyo.
10. Chen, R. H., C. Abate, and J. Blenis. 1993. Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase. Proc. Natl. Acad. Sci. USA 90:10952-10956.
11. Chen, R. H., C. Sarnecki, and J. Blenis. 1992. Nuclear localization and regulation of erk- and rsk-encoded protein kinases. Mol. Cell. Biol. 12:915-927.
12. Cheng, J. T., M. H. Cobb, and R. Baer. 1993. Phosphorylation of the TAL1 oncoprotein by the extracellular-signal-regulaled protein kinase ERK1. Mol. Cell. Biol. 13:801-808.
13. Cowley, S., H. Paterson, P. Kemp, and C. J. Marshall. 1994. Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH3T3 cells. Cell 77:841-852.
14. Crossley, M., and S. H. Orkin. 1994. Phosphorylation of the crythroid transcription factor GATA-1. J. Biol. Chem. 269:16589-16596.
15. Daga, A., J. E. Tighe, and F. Calabi. 1992. Leukaemia/Drosophila homology. Nature (London) 356:484.
16. Davis, R. J. 1993. The mitogen-activated protein kinase signal transduction pathway. J. Biol. Chem. 268:14553-14556.
17. Derijard, B., M. Hibi, I. H. Wu, T. Barrett, B. Su, T. Deng, M. Karin, and R. J. Daris. 1994. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76:1025-1037.
18. Deryard, B., J. Raingeand, T. Barrett, I. H. Wu, J. Han, R. J. Ulevitch, and R. J. Davis. 1995. Independent human MAP kinase signal transduction pathways defined by MEK and MKK isoforms. Science 267:682-685.
19. Erickson, P., J. Gao, K. S. Chang, T. Look, E. Whisenant, S. Raimondi, R. Lasher, J. Trujillo, J. Rowley, and H. Drabkin. 1992. Identification of breakpoints in t(8;21) acute myclogenous leukemia and isolation of a fusion transcript, AML1/ETO, with similarity to Drosophila segmentation gene, runt. Blood 80:1825-1831.
20. Erickson, P., M. Robinson, G. Owens, and H. A. Drabkin. 1994. The ETO portion of acute myeloid leukemia t(8;21) fusion transcript encodes a highly evolutionary conserved, putative transcription factor. Cancer Res. 54:1782-1786.
21. Frank, R., J. Zhang, H. Uchida, S. Meyers, S. W. Hiebert, and S. D. Nimer. 1995. The AML1/ETO fusion protein blocks transactivation of the GM-CSF promoter by AML1B. Oncogene 11:2667-274.
22. Furukawa, K., Y. Yamaguchi, E. Ogawa, K. Shigesada, M. Satake, and Y. Ito. 1990. A ubiquitous repressor interacting with an F9 cell-specific silencer and its functional suppression by differentiated cell-specific positive factors. Cell Growth Differ. 1:135-147.
23. Giese, K., C. Kingsley, J. R. Kirshner, and R. Grosschedl. 1995. Assembly and function of a TCRα enhancer complex is dependent on LEF-1-induced DNA bending and multiple protein-protein interactions. Genes Dev. 9:995-1008.
24. Golub, T. R., G. F. Barker, S. K. Bohlander, S. W. Hiebert, D. C. Ward, W. P. Bray, E. Morgan, S. C. Raimondi, J. D. Rowley, and D. G. Gilliland. 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.
25. Gonzalez, F. A., A. Seth, D. L. Raden, D. S. Bowman, F. S. Fay, and R. J. Davis. 1993. Serum-induced translocation of mitogen-activated protein kinase to the cell surface ruffling membrane and the nucleus. J. Cell. Biol. 122:1089-1101.
26. Gupta, S., and R. J. Davis. 1994. MAP kinase binds to the NH2-terminal activation domain of c-Myc. FEBS Lett. 353:281-285.
27. Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual, p. 421-510. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
28. Hattori, S., M. Fukuda, T. Yamashita, S. Nakamura, Y. Gotoh, and E. Nishida. 1992. Activation of mitogen-activated protein kinase and its activator by ras in intact cells and in a cell-free system. J. Biol. Chem. 267:20346-20351.
29. Hernandez, M. C., and M. S. Krangel. 1994. Regulation of the T-cell receptor δ enhancer by functional cooperation between c-Myb and corebinding factors. Mol. Cell. Biol. 14:473-483.
30. Hernandez, M. C., and M. S. Krangel. 1995. c-Myb and core-binding factor/PEBP2 display functional synergy but bind independently to adjacent sites in the T-cell receptor B enhancer. Mol. Cell. Biol. 15:3090-3099.
31. Hill, C. S., and R. Treisman. 1995. Transcriptional regulation by extracellular signals: mechanisms and specificity. Cell 80:199-211.
32. Hunter, T., and M. Karin. 1992. The regulation of transcription by phosphorylation. Cell 70:375-387.
33. Kagoshima, H., K. Shigesada, M. Satake, Y. Ito, H. Miyoshi, M. Ohki, M. Pepling, and P. Gergen. 1993. The Runt domain identifies a new family of heteromeric transcriptional regulators. Trends Genet. 9:338-341.
34. Kallunki, T., B. Su, I. Tsigelny, H. K. Sluss, B. Derijard, G. Moore, R. Davis, and M. Karin. 1994. JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation. Genes Dev. 8:2995-3007.
35. Karin, M. 1995. The regulation of AP-1 activity by mitogen-activated protein kinases. J. Biol. Chem. 270:16483-16486.
36. Khalil, R. A., C. B. Menice, C. L. Wang, and K. G. Morgan. 1995. Phosphotyrosine-dependent targeting of mitogen-activated protein kinase in differentiated contractile vascular cells. Circ. Res. 76:1101-1108.
37. Kharbanda, S., A. Saleem, Y. Emoto, R. Stone, U. Rapp, and D. Kufe. 1994. Activation of Raf-1 and mitogen-activated protein kinase during monocytic differentiation of human myeloid leukemia cells. J. Biol. Chem. 269:872-878.
38. Kinoshita, T., T. Yokota, K. Arai, and A. Miyajima. 1995. Suppression of apoptotic death in hematopoietic cells by signalling through the IL-3/GM-CSF receptors. EMBO J. 14:266-275.
39. Kolodziej, P. A., and R. A. Young. 1991. Epitope tagging and protein surveillance. Methods Enzymol. 194:508-519.
40. Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
41. Kurokawa, M., S. Ogawa, T. Tanaka, K. Mitani, Y. Yazaki, O. N. Witte, and H. Hirai. 1995. The AML1/Evi-1 fusion protein in the t(3;21) translocation exhibits transforming activity on Rat1 flbroblasts with dependence on Evi-1 sequence. Oncogene 11:833-840.
42. Kurokawa, M., T. Tanaka, K. Tanaka, S. Ogawa, K. Mitani, Y. Yazaki, and H. Hirai. 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.
43. LaBonne, C., B. Burke, and M. Whitman. 1995. Role of MAP kinase in mesoderm induction and axial patterning during Xenopus development. Development 121:1475-1486.
44. Lenormand, P., C. Sardet, G. Pages, G. L'Allemain, A. Brunet, and J. Pouyssegur. 1993. Growth factors induce nuclear translocation of MAP kinases (p42mapk and p44mapk) but not of their activator MAP kinase kinase (p45mapkk) in fibroblasts. J. Cell Biol. 122:1079-1088.
45. Levanon, D., V. Negreanu, Y. Bernstein, A. I. Bar, L. Avivi, and Y. Groner. 1994. AML1, AML2, and AML3, the human members of the runt domain gene-family: cDNA structure, expression, and chromosomal localization. Genomics 23:425-432.
46. Liu, P., S. A. Tarie, A. Hajra, D. F. Claxton, P. Marlton, M. Freedman, M. J. Siciliano, and F. S. Collins. 1993. Fusion between transcription factor CBFβ/PEBP2β and a myosin heavy chain in acute myeloid leukemia. Science 261:1041-1044.
47. Liu, P. P., A. Hajra, C. Wymenga, and F. S. Collins. 1995. Molecular pathogenesis of the chromosome 16 inversion in the M4Eo. Blood 85:2289-2302.
48. Lu, J., M. Maruyama, M. Satake, S. C. Bae, E. Ogawa, H. Kagoshima, K. Shigesada, and Y. Ito. 1995. Subcellular localization of the α and β subunits of the acute myeloid leukemia-linked transcription factor PEBP2/CBF. Mol. Cell. Biol. 15:1651-1661.
49. Marshall, C. J. 1995. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80:179-185.
50. Meyers, S., J. R. Downing, and S. W. Hiebert. 1993. Identification of AML-1 and the (8;21) translocation protein (AML-1/ETO) as sequence-specific DNA-binding proteins: the runt homology domain is required for DNA binding and protein-protein interactions. Mol. Cell. Biol. 13:6336-6345.
51. Meyers, S., N. Lenny, and S. W. Hiebert. 1995. The t(8;21) fusion protein interferes with AML-1B-dependent transcriptional activation. Mol. Cell. Biol. 15:1974-1982.
52. Minden, A., A. Lin, M. McMahon, C. Lange-Carter, B. Derijard, R. J. Davis, G. L. Johnson, and M. Karin. 1994. Differential activation of ERK and JNK mitogen-activated protein kinases by Raf-1 and MEKK. Science 266:1719-1723.
53. Mitani, K., S. Ogawa, T. Tanaka, H. Miyoshi, M. Kurokawa, H. Mano, Y. Yazaki, M. Ohki, and H. Hirai. 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.
54. Miyoshi, H., T. Kozu, K. Shimizu, K. Enomoto, N. Maseki, Y. Kaneko, N. Kamada, and M. Ohki. 1993. The t(8;21) translocation in acute myeloid leukemia results in production of an AML1-MTG8 fusion transcript. EMBO J. 12:2715-2721.
55. Miyoshi, H., M. Ohira, K. Shimizu, K. Mitani, H. Hirai, T. Imai, K. Yokoyama, E. Soeda, and M. Ohki. 1995. Alternative splicing and genomic structure of the AML1 gene involved in acute myeloid leukemia. Nucleic Acids Res. 23:2762-2769.
56. Miyoshi, H., K. Shimizu, T. Kozu, N. Maseki, Y. Kaneko, and M. Ohki. 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.
57. Muller, A. J., J. C. Young, A. M. Pendergast, M. Pondel, N. R. Landau, D. R. Littman, and O. N. Witte. 1991. BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias. Mol. Cell. Biol. 11:1785-1792.
58. Nuchprayoon, I., S. Meyers, L. M. Scott, J. Suzow, S. Hiebert and A. D. Friedman. 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.
59. Nucifora, G., C. R. Begy, P. Erickson, H. A. Drabkin, and J. D. Rowley. 1993. The 3;21 translocation in myelodysplasia results in a fusion transcript between the AML1 gene and the gene for EAP, a highly conserved protein associated with the Epstein-Barr virus small RNA EBER 1. Proc. Natl. Acad. Sci. USA 90:7784-7788.
60. Nucifora, G., C. R. Begy, H. Kobayashi, D. Roulston, D. Claxton, B. J. Pedersen, E. Parganas, J. N. Idle, and J. D. Rowley. 1994. Consistent intergenic splicing and production of multiple transcripts between AML1 at 21q22 and unrelated genes at 3q26 in (3:21)(q26;q22) translocations. Proc. Natl. Acad. Sci. USA 91:4004-4008.
61. Nucifora, G., D. J. Birn, R. Espinosa III, P. Erickson, M. M. LeBeau, D. Roulston, T. W. McKeithan, H. Drabkin, and J. D. Rowley. 1993. Involvement of the AML1 gene in the t(3;21) in therapy-related leukemia and in chronic myeloid leukemia in blast crisis. Blood 81:2728-2734.
62. Nucifora, G., and J. D. Rowley. 1995. AML1 and the 8;21 and 3;21 trans-locations in acute and chronic myeloid leukemia. Blood 86:1-14.
63. Ogawa, E., M. Inuzuka, M. Maruyama, M. Satake, F. M. Naito, Y. Itd, and K. Shigesada. 1993. Molecular cloning and characterization of PEBP2β, the heterodimeric partner of a novel Drosophila runt-related DNA binding protein PEBP2α. Virology 194:314-331.
64. Ogawa, E., M. Maruyama, L. F. Chen, Y. Murakami, and Y. Ito. 1995. Analysis of the mechanism of transcription activation by PEBP2, abstr. 713, p. 230. In Abstracts of the 54th Annual Meeting of the Japanese Cancer Association 1995. Japanese Cancer Association, Tokyo.
65. Ogawa, E., M. Maruyama, H. Kagoshima, M. Inuzuka, J. Lu, M. Satake, K. Shigesada, and Y. Ito. 1993. PEBP2/PEA2 represents a family of transcription factors homologous to the products of the Drosophila runt gene and the human AML1 gene. Proc. Natl. Acad. Sci. USA 90:6859-6863.
66. Ohki, M. 1993. Molecular basis of the t(8;21) translocation in acute myeloid leukaemia. Semin. Cancer Biol. 4:369-375.
67. Okazaki, K., and N. Sagata. 1995. The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH3T3 cells. EMBO J. 14:5048-5059.
68. Okazaki, K., and N. Sagata. 1995. MAP kinase activation is essential for oncogenic transformation of NIH3T3 cells by Mos. Oncogene 10:1149-1157.
69. Okuda, K., J. S. Sanghera, S. L. Pelech, Y. Kanakura, M. Hallek, J. D. Griffin, and B. J. Druker. 1992. Granulocyte-macrophage colony-stimulating factor, interleukin-3, and steel factor induce rapid tyrosine phosphorylation of p42 and p44 MAP kinase. Blood 79:2880-2887.
70. Okuda, T., J. Deursen, S. W. Hiebert, G. Grosbeld, and J. R. Downing. 1996. AMLl, the target of multiple chromosomal translocations in human leukemia, is essential for normal fetal liver hematopoiesis. Cell 84:321-330.
71. Pages, G., P. Lenormand, G. L'Allemain, J. C. Chambard, S. Meloche, and J. Pouyssegur. 1993. Mitogen-activated protein kinases p42mapk and p44mapk are requited for fibroblast proliferation. Proc. Natl. Acad. Sci. USA 90:8319-8323.
72. Pulverer, B. J., J. M. Kyriakis, J. Avruch, E. Nikolakaki, and J. R. Woodgett. 1991. Phosphorylation of c-jun mediated by MAP kinases. Nature (London) 353:670-674.
73. Rabault, B., and J. Ghysdael. 1994. Calcium-induced phosphorylation of ETS1 inhibits its specific DNA binding activity. J. Biol. Chem. 269:28143-18151.
74. Raingeaud, J., A. J. Whitmarsh, T. Barrett, B. Derijard, and R. J. Davis. 1996. MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway. Mol. Cell. Biol. 16:1247-1255.
75. Rao, V. N., and E. S. Reddy. 1994. Elk-1 proteins interact with MAP kinases. Oncogene 9:1855-1860.
76. Hobbins, D. J., E. Zhen, H. Owaki, C. A. Vanderbilt, D. Ebert, T. D. Geppert, and M. H. Cobb. 1993. Regulation and properties of extracellular signal-regulated protein kinases 1 and 2 in vitro. J. Biol. Chem. 268:5097-5106.
77. Romana, S. P., M. Mauchauffe, C. M. Le, I. Chumakov, P. D. Le, R. Berger, and O. A. Bernard. 1995. The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1 gene fusion. Blood 85:3662-3670.
78. Rudnicki, M. A., and M. W. McBurney. 1987. Cell culture methods and induction of differentiation of embryonal carcinoma cell lines, p. 19-49. In E. J. Robertson (ed.), Teratocarcinomas and embryonic stem cells. IRL Press, Oxford.
79. Rutberg, S. E., L. R. Dolan, and Z. Ronai. 1994. PEBP2 - a modulator of polyoma DNA replication. DNA Cell Biol. 13:865-874.
80. Sakakura, C., I. Y. Yamaguchi, M. Satake, S. C. Bae, A. Takahashi, E. Ogawa, A. Hagiwara, T. Takahashi, A. Murakami, K. Makino, T. Nakagawa, N. Kanada and Y. Ito. 1994. Growth inhibition and induction of differentiation of t(8;21) acute myeloid leukemia cells by the DNA-binding domain of PEBP2 and the AML1/MTG8(ETO)-specific antisense oligonucleotide. Proc. Natl. Acad. Sci. USA 91:11723-11727.
81. Satake, M., S. Nomura, I. Y. Yamaguchi, Y. Takahama, Y. Hashimoto, M. Niki, Y. Kitamura, and Y. Ito. 1995. Expression of the Runt domain-encoding PEBP2a genes in T cells during thymic development. Mol. Cell. Biol. 15:1662-1670.
82. Sato, N., K. Sakamaki, N. Terada, K. Arai, and A. Miyajima. 1993. Signal transduction by the high-affinity GM-CSF receptor: two distinct cytoplasmic regions of the common β subunit responsible for different signaling. EMBO J. 12:4181-4189.
83. Shirakabe, K., Y. Gotoh, and E. Nishida, 1992. A mitogen-activated protein (MAP) kinase activating factor in mammalian mitogen-stimulated cells is homologous to Xenopus M phase MAP kinase activator. J. Biol. Chem. 267:16685-16690.
84. Sun, W., B. J. Graves, and N. A. Speck. 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.
85. Takahashi, A., M. Satake, I. Y. Yamaguchi, S. C. Bae, J. Lu, M. Maruyama, Y. W. Zhang, H. Oka, N. Arai, K. Arai, and Y. Ito. 1995. Positive and negative regulation of granulocyte-macrophage colony-stimulating factor promoter activity by AML1-related transcription factor, PEBP2. Blood 86:607-616.
86. Tanaka, K., T. Tanaka, S. Ogawa, M. Kurokawa, K. Mitani, Y. Yazaki, and H. Hirai. 1995. Increased expression of AML1 during retinoic-acid-induced differentiation of U937 cells. Biochem. Biophys. Res. Commun. 211:1023-1030.
87. Tanaka, T., K. Mitani, M. Kurokawa, S. Ogawa, K. Tanaka, J. Nishida, Y. Yazaki, Y. Shibata, and H. Hirai. 1995. Dual functions of the AML1/Evi-1 chimeric protein in the mechanism of leukemogenesis in t(3;21) leukemias. Mol. Cell. Biul. 15:2383-2392.
88. Tanaka, T., J. Nishida, K. Mitani, S. Ogawa, Y. Yazaki, and H. Hirai. 1994. Evi-1 raises AP-1 activily and stimulates c-fos promoter transactivation with dependence or the second zinc finger domain. J. Biol. Chem. 269:24020-24026.
89. Tanaka, T., K. Tanaka, M. Kurokawa, and H. Hirai. Unpublished data.
90. Tanaka, T., K. Tanaka, S. Ogawa, M. Kurokawa, K. Mitani, J. Nishida, Y. Shibata, Y. Yazaki, and H. Hirai. 1995. An acute myeloid leukemia gene, AML1, regulates hematopoietic myeloid cell differentiation and transcriptional activation antagonistically by two alternative spliced forms. EMBO J. 14:341-350.
91. Tobe, K., T. Kadowaki, H. Tamemoto, K. Ueki, K. Hara, O. Koshio, K. Momomura, Y. Gotoh, E. Nishida, Y. Akanuma, Y. Yazaki, and M. Kasuga. 1991. Insulin and 12-O-tetradecanoylphorbol-13-acetate activation of two immunologically distinct myelin basic protein/microtubule-associated protein 2 (MBP/MAP2) kinases via de novo phosphorylation of threonine and tyrosine residues. J. Biol. Chem. 266:24793-24803.
92. Towatari, M., G. E. May, R. Marais, G. R. Perkins, C. J. Marshall, S. Cowley, and T. Enver. 1995. Regulation of GATA-2 phosphorylation by mitogen-activated protein kinase and interleukin-3. J. Biol. Chem. 270:4101-4107.
93. Ueki, K., S. Matsuda, K. Tobe, Y. Gotoh, H. Tamemnto, M. Yachi, Y. Akanuma, Y. Yazaki, E. Nishida, and T. Kadowaki. 1994. Feedback regulation of mitogen-activated protein kinase kinase kinase activity of c-Raf-1 by insulin and phorbol ester stimulation. J. Biol. Chem. 269:15756-15761.
94. Wang, S., Q. Wang, B. E. Crate, I. N. Melnikova, S. R. Keller, and N. A. Speck. 1993. Cloning and characterization of subunits of the T-cell receptor and murine leukemia virus enhancer core-binding factor. Mol. Cell. Biol. 13:3324-3339.
95. Wang, S. W., and N. A. Speck. 1992. Purification of core-binding factor, a protein that binds the conserved core site in murine leukemia virus enhancers. Mol. Cell. Biol. 12:89-102.
96. Wijmenga, C., N. A. Speck, N. C. Dracopoli, M. H. Hofker, P. Liu, and F. S. Collins. 1995. Identification of a new murine runt domain-containing gene, Cbfa3. Genomics 26:611-614.
97. Wotton, D., J. Ghysdael, S. Wang, N. A. Speck, and M. J. Owen. 1994. Cooperative binding of Ets-1 and core binding factor to DNA. Mol. Cell. Biol. 14:840-850.
98. Zaiman, A. L., A. F. Lewis, B. E. Crute, N. A. Speck, and J. Lenz. 1995. Transcriptional activity of core binding factor α (AML1) and β subunits on murine leukemia virus enhancer cores. J. Virol. 69:2898-2906.
99. Zhang, D. E., K. Fujioka, C. J. Hetherington, L. H. Shapiro, H. M. Chen, A. T. Look, and D. G. Tenen. 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.
100. Zhang, D. E., C. J. Hetherington, S. Meyers, K. L. Rhoades, C. J. Larson, H. M. Chen, S. W. Hiebert, and D. G. Tenen. 1996. CCAAT enhancer-binding protein (C/EBP) and AML1 (CBFα2) synergistically activate the macrophage colony-stimulating factor receptor promoter. Mol. Cell. Biol. 16:1231-1240.
101. Zhang, Y., S. Moreland, and R. S. Moreland. 1994. Regulation of vascular smooth muscle contraction: myosin light chain phosphorylation dependent and independent pathways. Can. J. Physiol. Pharmacol. 72:1386-1391.
102. Zhu, X., J. E. Yeadon, and S. J. Burden. 1994. AML1 is expressed in skeletal muscle and is regulated by innervation. Mol. Cell. Biol. 14:8051-8057.