메뉴 건너뛰기




Volumn 90, Issue 1, 1999, Pages 60-68

Association of MTG8 (ETO/CDR), a leukemia-related protein, with serine/threonine protein kinases and heat shock protein HSP90 in human hematopoietic cell lines

Author keywords

Leukemogenesis; MTG8C kinase; MTG8N kinase

Indexed keywords

HEAT SHOCK PROTEIN 90; ONCOPROTEIN; PROTEIN SERINE THREONINE KINASE; RECOMBINANT PROTEIN;

EID: 0033005390     PISSN: 09105050     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1349-7006.1999.tb00666.x     Document Type: Article
Times cited : (12)

References (37)
  • 1
    • 0021593913 scopus 로고
    • Biological implications of consistent chromosome rearrangements in leukemia and lymphoma
    • Rowley, J. D. Biological implications of consistent chromosome rearrangements in leukemia and lymphoma. Cancer Res., 44, 3159-3168 (1984).
    • (1984) Cancer Res. , vol.44 , pp. 3159-3168
    • Rowley, J.D.1
  • 2
    • 0025746321 scopus 로고
    • t(8:21) breakpoints on chromosome 21 in acute myeloid leukemia are clustered within a limited region of a single gene
    • Miyoshi, H., Shimizu, K., Kozu, T., Museki, N., Kaneko, Y. and Ohki, M. 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 (1991).
    • (1991) AML1. Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10431-10434
    • Miyoshi, H.1    Shimizu, K.2    Kozu, T.3    Museki, N.4    Kaneko, Y.5    Ohki, M.6
  • 3
    • 0026757174 scopus 로고
    • Identification of breakpoints in t(8;21) acute myelogenous leukemia and isolation of a fusion transcript, AML1/ETO, with similarity to drosophila segmentation gene, runt
    • Erickson, P., Gao, J., Chang, K.-S., Look, T., Whisenant, E., Raimondi, S., Lasher, R., Trujillo, J., Rowley, J. and Drabkin, H. Identification of breakpoints in t(8;21) acute myelogenous leukemia and isolation of a fusion transcript, AML1/ETO, with similarity to Drosophila segmentation gene, runt. Blood, 80, 1825-1831 (1992).
    • (1992) Blood , vol.80 , pp. 1825-1831
    • Erickson, P.1    Gao, J.2    Chang, K.-S.3    Look, T.4    Whisenant, E.5    Raimondi, S.6    Lasher, R.7    Trujillo, J.8    Rowley, J.9    Drabkin, H.10
  • 4
    • 0027265454 scopus 로고
    • Junctions of the AML1/MTG8 (ETO) fusion are constant in t(8;21) acute myeloid leukemia detected by reverse transcription polymerase chain reaction
    • Kozu, T., Miyoshi, H., Shimizu, K., Maseki, N., Kaneko, Y., Asou, H., Kamada, N. and Ohki, M. Junctions of the AML1/MTG8 (ETO) fusion are constant in t(8;21) acute myeloid leukemia detected by reverse transcription polymerase chain reaction. Blood, 82, 1270-1276 (1993).
    • (1993) Blood , vol.82 , pp. 1270-1276
    • Kozu, T.1    Miyoshi, H.2    Shimizu, K.3    Maseki, N.4    Kaneko, Y.5    Asou, H.6    Kamada, N.7    Ohki, M.8
  • 5
    • 0027218725 scopus 로고
    • The t(8;21) translocation in acute myeloid leukemia results in production of an AML1-MTG8 fusion transcript
    • Miyoshi, H., Kozu, T., Shimizu, K., Enomoto, K., Maseki, N., Kaneko, Y., Kamada, N. and Ohki, M. The t(8;21) translocation in acute myeloid leukemia results in production of an AML1-MTG8 fusion transcript. EMBO J., 12, 2715-2721 (1993).
    • (1993) EMBO J. , vol.12 , pp. 2715-2721
    • Miyoshi, H.1    Kozu, T.2    Shimizu, K.3    Enomoto, K.4    Maseki, N.5    Kaneko, Y.6    Kamada, N.7    Ohki, M.8
  • 7
    • 0028925282 scopus 로고
    • The t(8;21) fusion protein interferes with AML-1B-dependent transcriptional activation
    • Meyers, S., Lenny, N. and Hiebert, S. W. The t(8;21) fusion protein interferes with AML-1B-dependent transcriptional activation. Mol. Cell. Biol., 15, 1974-1982 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1974-1982
    • Meyers, S.1    Lenny, N.2    Hiebert, S.W.3
  • 8
    • 0029616633 scopus 로고
    • The AML1/ETO fusion protein blocks transactivation of the GM-CSF promoter by AML1B
    • Frank, R., Zhang, J., Uchida, H., Meyers, S., Hiebert, S. W. and Nimer, S. D. The AML1/ETO fusion protein blocks transactivation of the GM-CSF promoter by AML1B. Oncogene, 11, 2667-2674 (1995).
    • (1995) Oncogene , vol.11 , pp. 2667-2674
    • Frank, R.1    Zhang, J.2    Uchida, H.3    Meyers, S.4    Hiebert, S.W.5    Nimer, S.D.6
  • 9
    • 0028786125 scopus 로고
    • Functional domains of the t(8;21) fusion protein, AML-1/ETO
    • Lenny, N., Meyers, S. and Hiebert, S. W. Functional domains of the t(8;21) fusion protein, AML-1/ETO. Oncogene, 11, 1761-1769 (1995).
    • (1995) Oncogene , vol.11 , pp. 1761-1769
    • Lenny, N.1    Meyers, S.2    Hiebert, S.W.3
  • 10
    • 0031972701 scopus 로고    scopus 로고
    • The t(8;21) fusion product, AML-1-ETO, associates with C/EBP-α, inhibits C/EBP-α-dependent transcription, and blocks granulocytic differentiation
    • Westendorf, J. J., Yaniamoto, C. M., Lenny, N., Downing, J. R., Selsted, M. E. and Hiebert, S. W. The t(8;21) fusion product, AML-1-ETO, associates with C/EBP-α, inhibits C/EBP-α-dependent transcription, and blocks granulocytic differentiation. Mol. Cell. Biol., 18, 322-333 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 322-333
    • Westendorf, J.J.1    Yaniamoto, C.M.2    Lenny, N.3    Downing, J.R.4    Selsted, M.E.5    Hiebert, S.W.6
  • 11
    • 0029859199 scopus 로고    scopus 로고
    • Synergistic up-regulation of the myeloid-specific promoter for the macrophage colony-stimulating factor receptor by AML1 and the t(8:21) fusion protein may contribute to leukemogenesis
    • Rhoades, K. L., Hetherington, C. J., Rowley, J. D., Hiebert, S. W., Nucifora, G., Tenen, D. G. and Zhang, D.-E. Synergistic up-regulation of the myeloid-specific promoter for the macrophage colony-stimulating factor receptor by AML1 and the t(8:21) fusion protein may contribute to leukemogenesis. Proc. Natl. Acad. Sci. USA, 93, 11895-11900 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11895-11900
    • Rhoades, K.L.1    Hetherington, C.J.2    Rowley, J.D.3    Hiebert, S.W.4    Nucifora, G.5    Tenen, D.G.6    Zhang, D.-E.7
  • 13
    • 0028267241 scopus 로고
    • The ETO portion of acute myeloid leukemia t(8:21) fusion transcript encodes a highly evolutionary conserved, putative transcription factor
    • Erickson, P. F., Robinson, M., Owens, G. and Drabkin, H. A. 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 (1994).
    • (1994) Cancer Res. , vol.54 , pp. 1782-1786
    • Erickson, P.F.1    Robinson, M.2    Owens, G.3    Drabkin, H.A.4
  • 14
    • 0028990261 scopus 로고
    • Identification of two transcripts of AML1/ ETO-fused gene in t(8;21) leukemic cells and expression of wild-type ETO gene in hematopoietic cells
    • Era, T., Asou, N., Kunisada, T., Yamasaki, H., Asou, H., Kamada, N., Nishikawa, S.-I., Yamaguchi, K. and Takatsuki, K. Identification of two transcripts of AML1/ ETO-fused gene in t(8;21) leukemic cells and expression of wild-type ETO gene in hematopoietic cells. Genes Chromosom. Cancer, 13, 25-33 (1995).
    • (1995) Genes Chromosom. Cancer , vol.13 , pp. 25-33
    • Era, T.1    Asou, N.2    Kunisada, T.3    Yamasaki, H.4    Asou, H.5    Kamada, N.6    Nishikawa, S.-I.7    Yamaguchi, K.8    Takatsuki, K.9
  • 16
    • 0031858792 scopus 로고    scopus 로고
    • Tumourigenicity of MTG8, a leukaemia-related gene, in concert with v-Ha-ras gene in BALB/3T3 cells
    • Sueoka, E., Sueoka, N., Okabe, S., Komori, A., Suganuma, M., Kozu, T. and Fujiki, H. Tumourigenicity of MTG8, a leukaemia-related gene, in concert with v-Ha-ras gene in BALB/3T3 cells. Br. J. Haematol., 101, 737-742 (1998).
    • (1998) Br. J. Haematol. , vol.101 , pp. 737-742
    • Sueoka, E.1    Sueoka, N.2    Okabe, S.3    Komori, A.4    Suganuma, M.5    Kozu, T.6    Fujiki, H.7
  • 17
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell, D. A. and Lindquist, S. The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Genet., 21, 437-496 (1993).
    • (1993) Annu. Rev. Genet. , vol.21 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 18
    • 0025817842 scopus 로고
    • Establishment of a human acute myeloid leukemia cell line (Kasumi-1) with 8:21 chromosome translocation
    • Asou, H., Tashiro, S., Hamamoto, K., Otsuji, A., Kita, K. and Kamuda, N. Establishment of a human acute myeloid leukemia cell line (Kasumi-1) with 8:21 chromosome translocation. Blood, 77, 2031-2036 (1991).
    • (1991) Blood , vol.77 , pp. 2031-2036
    • Asou, H.1    Tashiro, S.2    Hamamoto, K.3    Otsuji, A.4    Kita, K.5    Kamuda, N.6
  • 20
    • 0027423418 scopus 로고
    • Identification of an oncoprotein-and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain
    • Hibi, M., Lin, A., Smeal, T., Minden, A. and Karin, M. Identification of an oncoprotein-and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes Dev., 7, 2135-2148 (1993).
    • (1993) Genes Dev. , vol.7 , pp. 2135-2148
    • Hibi, M.1    Lin, A.2    Smeal, T.3    Minden, A.4    Karin, M.5
  • 21
    • 0024558784 scopus 로고
    • Acid and base hydrolysis of phosphoproteins bound to immobilon facilitates analysis of phosphoamino acids in gel-fractionated proteins
    • Kamps, M. P. and Sefton, B. M. Acid and base hydrolysis of phosphoproteins bound to immobilon facilitates analysis of phosphoamino acids in gel-fractionated proteins. Anal. Biochem., 176, 22-27 (1989).
    • (1989) Anal. Biochem. , vol.176 , pp. 22-27
    • Kamps, M.P.1    Sefton, B.M.2
  • 22
    • 0027221568 scopus 로고
    • γ-Phosphate-linked ATP-sepharose for the affinity purification of protein kinases. Rapid purification to homogeneity of skeletal muscle mitogen-activated protein kinase kinase
    • Haystead, C. M. M., Gregory, P., Sturgill, T. W. and Haystead, T. A. J. γ-Phosphate-linked ATP-Sepharose for the affinity purification of protein kinases. Rapid purification to homogeneity of skeletal muscle mitogen-activated protein kinase kinase. Eur. J. Biochem., 214, 459-467 (1993).
    • (1993) Eur. J. Biochem. , vol.214 , pp. 459-467
    • Haystead, C.M.M.1    Gregory, P.2    Sturgill, T.W.3    Haystead, T.A.J.4
  • 23
    • 0024358172 scopus 로고
    • Sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel
    • Kameshita, I. and Fujisawa, H. A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel. Anal. Biochem., 183, 139-143 (1989).
    • (1989) Anal. Biochem. , vol.183 , pp. 139-143
    • Kameshita, I.1    Fujisawa, H.A.2
  • 24
    • 0027272945 scopus 로고
    • Tumor promotion by inhibitors of protein phosphatases 1 and 2A: The okadaic acid class of compounds
    • Fujiki, H. and Suganuma, M. Tumor promotion by inhibitors of protein phosphatases 1 and 2A: the okadaic acid class of compounds. Adv. Cancer Res., 61, 143-194 (1993).
    • (1993) Adv. Cancer Res. , vol.61 , pp. 143-194
    • Fujiki, H.1    Suganuma, M.2
  • 25
    • 0023224123 scopus 로고
    • Nucleolide sequence of a cDNA for a member of the human 90 kDa heat-shock protein family
    • Rebbe, N. F., Ware, J., Bertina, R. M. Modrich P. and Stafford, D. W. Nucleolide sequence of a cDNA for a member of the human 90 kDa heat-shock protein family. Gene, 53, 235-245 (1987).
    • (1987) Gene , vol.53 , pp. 235-245
    • Rebbe, N.F.1    Ware, J.2    Bertina, R.M.3    Modrich, P.4    Stafford, D.W.5
  • 26
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou, C., Poe, S. M. O'Brien, R., Ladbury, J. E., Piper, P. W. and Pearl, L. H. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell, 90, 65-75 (1997).
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Poe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 27
    • 0029986957 scopus 로고    scopus 로고
    • DHAF-1, a novel protein that binds an essential region in a deformed response element
    • Gross, C. T. and McGinnins, W. DHAF-1, a novel protein that binds an essential region in a Deformed response element. EMBO J., 15, 1961-1970 (1996).
    • (1996) EMBO J. , vol.15 , pp. 1961-1970
    • Gross, C.T.1    McGinnins, W.2
  • 29
    • 0031844689 scopus 로고    scopus 로고
    • The MYND motif is required for repression of basal transcription from the multidrug resistance 1 promoter by the t(8;21) fusion protein
    • Lutterbach, B., Sun, D., Schuetz, S. D. and Hiebert, S. W. The MYND motif is required for repression of basal transcription from the multidrug resistance 1 promoter by the t(8;21) fusion protein. Mol. Cell. Biol., 18, 3604-3611 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3604-3611
    • Lutterbach, B.1    Sun, D.2    Schuetz, S.D.3    Hiebert, S.W.4
  • 30
    • 0031895351 scopus 로고    scopus 로고
    • The hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors
    • Pratt, W. B. The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc. Soc. Exp. Biol. Med., 217, 420-434 (1998).
    • (1998) Proc. Soc. Exp. Biol. Med. , vol.217 , pp. 420-434
    • Pratt, W.B.1
  • 32
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins, C. E., Russo, A. A., Schneider, C., Rosen, N., Hartl, F. U. and Pavletich, N. P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell. 89, 239-250 (1997).
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 33
  • 35
    • 0029973294 scopus 로고    scopus 로고
    • Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
    • Whitesell, L. and Cook, P. Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. Mol. Endocrinol., 10, 705-712 (1996).
    • (1996) Mol. Endocrinol. , vol.10 , pp. 705-712
    • Whitesell, L.1    Cook, P.2
  • 37


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.