Cited by 368Acute Myeloid Leukemia ResearchRetinoids in leukemia and cellular processesGenomics and Chromatin Dynamics

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The t(8;21) Fusion Protein Interferes with AML-1B-Dependent Transcriptional Activation

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Meyers, Shari, Lenny, Noel, Hiebert, Scott W.·1995·Molecular and Cellular Biology

DOI 10.1128/mcb.15.4.1974PMC PMC230424

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Abstract

The AML-1/CBF beta transcription factor complex is targeted by both the t(8;21) and the inv(16) chromosomal alterations, which are frequently observed in acute myelogenous leukemia. AML-1 is a site-specific DNA-binding protein that recognizes the enhancer core motif TGTGGT. The t(8;21) translocation fuses the first 177 amino acids of AML-1 to MTG8 (also known as ETO), generating a chimeric protein that retains the DNA-binding domain of AML-1. Analysis of endogenous AML-1 DNA-binding complexes suggested the presence of at least two AML-1 isoforms. Accordingly, we screened a human B-cell cDNA library and isolated a larger, potentially alternatively spliced, form of AML1, termed AML1B. AML-1B is a protein of 53 kDa that binds to a consensus AML-1-binding site and complexes with CBF beta. Subcellular fractionation experiments demonstrated that both AML-1 and AML-1/ETO are efficiently extracted from the nucleus under ionic conditions but that AML-1B is localized to a salt-resistant nuclear compartment. Analysis of the transcriptional activities of AML-1, AML-1B, and AML-1/ETO demonstrated that only AML-1B activates transcription from the T-cell receptor beta enhancer. Mixing experiments indicated that AML-1/ETO can efficiently block AML-1B-dependent transcriptional activation, suggesting that the t(8;21) translocation creates a dominant interfering protein.

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Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,262
Recombinant Genomes Which Express Chloramphenicol Acetyltransferase in Mammalian Cells
Gorman, C., Moffat, L. F., & Howard, B. H. (1982) · Molecular and Cellular Biology · doi:10.1128/mcb.2.9.1044 · Cited by 7,674
The scanning model for translation: an update.
Kozak, M. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.2.229 · Cited by 3,485
t(8;21) breakpoints on chromosome 21 in acute myeloid leukemia are clustered within a limited region of a single gene, AML1.
Miyoshi, H., Shimizu, K., Kozu, T., Maseki, N., Kaneko, Y., & Ohki, M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10431 · Cited by 872
Multiple Point Mutations Affecting the Simian Virus 40 Enhancer
Weiher, H., König, M., & Gruß, P. (1983) · Science · doi:10.1126/science.6297005 · Cited by 803
Fusion Between Transcription Factor CBFβ/PEBP2β and a Myosin Heavy Chain in Acute Myeloid Leukemia
Liu, P., Tarlé, S. A., Hajra, A., Claxton, D. F., Marlton, P., Freedman, M., Siciliano, M. J., & Collins, F. S. (1993) · Science · doi:10.1126/science.8351518 · Cited by 732
Secreted placental alkaline phosphatase: a powerful new quantitative indicator of gene expression in eukaryotic cells
Berger, J., Hauber, J., Hauber, R., Geiger, R. E., & Cullen, B. R. (1988) · Gene · doi:10.1016/0378-1119(88)90219-3 · Cited by 667
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., Look, T., Whisenant, E., Raimondi, S., Lasher, R., Trujillo, J., Rowley, J., & Drabkin, H. (1992) · Blood · doi:10.1182/blood.v80.7.1825.1825 · Cited by 631
PEBP2/PEA2 represents a family of transcription factors homologous to the products of the Drosophila runt gene and the human AML1 gene.
Ogawa, E., Maruyama, M., Kagoshima, H., Inuzuka, M., Lu, J., Satake, M., Shigesada, K., & Ito, Y. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6859 · Cited by 608
The interaction of RB with E2F coincides with an inhibition of the transcriptional activity of E2F.Preprint
Hiebert, S. W., Chellappan, S., Horowitz, J. M., & Nevins, J. R. (1992) · Genes & Development · doi:10.1101/gad.6.2.177 · Cited by 576
Self-citation

Show all 46 references

Research works printed but not linked: 5

Bae S.-C., 1994, Mol. Cell. Biol., 14, 3242
Bae S. C., 1993, Oncogene, 8, 809
Gottschalk L. R., 1990, Mol. Cell. Biol., 10, 5486
Redondo J. M., 1991, Mol. Cell. Biol., 11, 5671
Wang S., 1993, EMBO J., 13, 3324

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Untitled work
(1999) · PubMed · Cited by 194
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Expression of the human acute myeloid leukemia gene AML1 is regulated by two promoter regions.
Ghozi, M. C., Bernstein, Y., Negreanu, V., Levanon, D., & Groner, Y. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.5.1935 · Cited by 150
The ETO Protein Disrupted in t(8;21)-Associated Acute Myeloid Leukemia Is a Corepressor for the Promyelocytic Leukemia Zinc Finger Protein
Melnick, A. M., Westendorf, J. J., Polinger, A., Carlile, G. W., Arai, S., Ball, H. J., Lutterbach, B. A., Hiebert, S. W., & Licht, J. D. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.6.2075-2086.2000 · Cited by 153
Self-citation
The AML1-MTG8 Leukemic Fusion Protein Forms a Complex with a Novel Member of the MTG8(ETO/CDR) Family, MTGR1
Kitabayashi, I., Ida, K., Morohoshi, F., Yokoyama, A., Mitsuhashi, N., Shimizu, K., Nomura, N., Hayashi, Y., & Ohki, M. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.2.846 · Cited by 153
The Runx genes: lineage-specific oncogenes and tumor suppressors
Cameron, E. R., & Neil, J. C. (2004) · Oncogene · doi:10.1038/sj.onc.1207130 · Cited by 154
Auto-Inhibition and Partner Proteins, Core-Binding Factor β (CBFβ) and Ets-1, Modulate DNA Binding by CBFα2 (AML1)
Gu, T.-L., Goetz, T. L., Graves, B. J., & Speck, N. A. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.1.91-103.2000 · Cited by 150
AML1-ETO Inhibits Maturation of Multiple Lymphohematopoietic Lineages and Induces Myeloblast Transformation in Synergy with ICSBP Deficiency
Schwieger, M., Löhler, J., Friel, J., Scheller, M., Horak, I. D., & Stocking, C. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20020824 · Cited by 143
The Runx1/AML1 transcription factor selectively regulates development and survival of TrkA nociceptive sensory neurons
Marmigère, F., Montelius, A., Wegner, M., Groner, Y., Reichardt, L. F., & Ernfors, P. (2006) · Nature Neuroscience · doi:10.1038/nn1631 · Cited by 141
Molecular mechanisms of ETS transcription factor-mediated tumorigenesis
Kar, A., & Gutierrez‐Hartmann, A. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.838202 · Cited by 151
Genomic structure and isoform expression of the mouse, rat and human Cbfa1/Osf2 transcription factor
Xiao, Z., Thomas, R. F., Hinson, T. K., & Quarles, L. D. (1998) · Gene · doi:10.1016/s0378-1119(98)00227-3 · Cited by 141
The Osteoblast Transcription Factor Runx2 Is Expressed in Mammary Epithelial Cells and Mediates osteopontin Expression
Inman, C. K., & Shore, P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308001200 · Cited by 140
The Leukemic Protein Core Binding Factor β (CBFβ)–Smooth-Muscle Myosin Heavy Chain Sequesters CBFα2 into Cytoskeletal Filaments and Aggregates
Adya, N., Stacy, T., Speck, N. A., & Liu, P. P. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7432 · Cited by 136
Recruitment of the nuclear receptor corepressor N-CoR by the TEL moiety of the childhood leukemia–associated TEL-AML1 oncoprotein
Guidez, F., Petrie, K. R., Ford, A. M., Lu, H., Bennett, C. A., MacGregor, A., Hannemann, J., Ito, Y., Ghysdael, J., Greaves, M. F., et al. (2000) · Blood · doi:10.1182/blood.v96.7.2557 · Cited by 134
Control of histone modifications
Davie, J., & Spencer, V. A. (1999) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(1999)75:32+ · Cited by 146
Self-citation
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., & Zhang, D. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11895 · Cited by 129
Self-citation
Functional and Physical Interactions between AML1 Proteins and an ETS Protein, MEF: Implications for the Pathogenesis of t(8;21)-Positive Leukemias
Mao, S. S., Frank, R. C., Zhang, J. C., Miyazaki, Y., & Nimer, S. D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3635 · Cited by 129
A Genetic Basis of Susceptibility to Acute Pyelonephritis
Lundstedt, A.-C., McCarthy, S., Gustafsson, M. C. U., Godaly, G., Jodal, U., Karpman, D., Leijonhufvud, I., Lindén, C., Martinell, J., Ragnarsdóttir, B., et al. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000825 · Cited by 127
Gfi‐1 attaches to the nuclear matrix, associates with ETO (MTG8) and histone deacetylase proteins, and represses transcription using a TSA‐sensitive mechanism
McGhee, L., Bryan, J., Elliott, L. T., Grimes, H. L., Kazanjian, A. A., Davis, J. N., & Meyers, S. (2003) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10548 · Cited by 122
Self-citation
TLE, the Human Homolog of Groucho, Interacts with AML1 and Acts as a Repressor of AML1-Induced Transactivation
Imai, Y., Kurokawa, M., Tanaka, K., Friedman, A. D., Ogawa, S., Mitani, K., Yazaki, Y., & Hirai, H. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9705 · Cited by 121
The inv(16) encodes an acute myeloid leukemia 1 transcriptional corepressor
Lutterbach, B. A., Hou, Y., Durst, K. L., & Hiebert, S. W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12822 · Cited by 122
Self-citation
Distinct roles for P-CREB and LEF-1 in TCR alpha enhancer assembly and activation on chromatin templates in vitro.
Mayall, T. P., Sheridan, P. L., Montminy, M. R., & Jones, K. A. (1997) · Genes & Development · doi:10.1101/gad.11.7.887 · Cited by 118
The expression of ETV6/CBFA2 (TEL/AML1) is not sufficient for the transformation of hematopoietic cell lines in vitro or the induction of hematologic disease in vivo
Andreasson, P., Schwaller, J., Anastasiadou, E., Aster, J. C., & Gilliland, D. G. (2001) · Cancer Genetics and Cytogenetics · doi:10.1016/s0165-4608(01)00518-0 · Cited by 121
AML1-ETO rapidly induces acute myeloblastic leukemia in cooperation with the Wilms tumor gene, WT1
Nishida, S., Hosen, N., Shirakata, T., Kanato, K., Yanagihara, M., Nakatsuka, S., Hoshida, Y., Nakazawa, T., Harada, Y., Tatsumi, N., et al. (2005) · Blood · doi:10.1182/blood-2005-04-1656 · Cited by 118
A role for RUNX1 in hematopoiesis and myeloid leukemia
Ichikawa, M., Yoshimi, A., Nakagawa, M. M., Nishimoto, N., Watanabe‐Okochi, N., & Kurokawa, M. (2013) · International Journal of Hematology · doi:10.1007/s12185-013-1347-3 · Cited by 118
Cell-Type-Dependent Up-Regulation of In Vitro Mineralization After Overexpression of the Osteoblast-Specific Transcription Factor Runx2/Cbfa1
Byers, B. A., Pavlath, G. K., Murphy, T. J., Karsenty, G., & Garcı́a, A. J. (2002) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2002.17.11.1931 · Cited by 114
Transcriptional co-repressors of Runx2
Westendorf, J. J. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20805 · Cited by 114
AML1 Is Functionally Regulated through p300-mediated Acetylation on Specific Lysine Residues
Yamaguchi, Y., Kurokawa, M., Imai, Y., Izutsu, K., Asai, T., Ichikawa, M., Yamamoto, G., Nitta, E., Yamagata, T., Sasaki, K., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400355200 · Cited by 112
The molecular signature of oncofusion proteins in acute myeloid leukemia
Martens, J. H. A., & Stunnenberg, H. G. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.04.002 · Cited by 111
Oligomerization of ETO Is Obligatory for Corepressor Interaction
Zhang, J., Hug, B. A., Huang, E. Y., Chen, C. W., Gelmetti, V., Maccarana, M., Minucci, S., Pelicci, P. G., & Lazar, M. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.1.156-163.2001 · Cited by 104
CBF alpha3 (AML2) is induced by TGF-beta1 to bind and activate the mouse germline Ig alpha promoter.
Shi, M. J., & Stavnezer, J. (1998) · PubMed · Cited by 105
Heterogeneity in CBF beta/MYH11 fusion messages encoded by the inv(16)(p13q22) and the t(16;16)(p13;q22) in acute myelogenous leukemia
Shurtleff, S., Meyers, S., Hiebert, S., Raimondi, S., Head, D., Willman, C., Wolman, S., Slovak, M., Carroll, A., & Behm, F. (1995) · Blood · doi:10.1182/blood.v85.12.3695.bloodjournal85123695 · Cited by 102
Self-citation
MLL-AFX Requires the Transcriptional Effector Domains of AFX To Transform Myeloid Progenitors and Transdominantly Interfere with Forkhead Protein Function
So, C. W. E., & Cleary, M. L. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.18.6542-6552.2002 · Cited by 101
CBFα3 (AML2) Is Induced by TGF-β1 to Bind and Activate the Mouse Germline Ig α Promoter
Shi, M., & Stavnezer, J. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.12.6751 · Cited by 115
Expression of the AML-1 Oncogene Shortens the G1Phase of the Cell Cycle
Strom, D. K., Nip, J., Westendorf, J. J., Linggi, B. E., Lutterbach, B. A., Downing, J. R., Lenny, N. T., & Hiebert, S. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3438 · Cited by 100
Self-citation

Authors: Meyers, S., Lenny, N., & Hiebert, S. W.
Affiliations: St. Jude Children's Research Hospital (US)
ORCID: Hiebert, Scott W.
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 1995-04-01
Volume: 15
Issue: 4
Pages: 1974-1982
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.15.4.1974
PMC: PMC230424
OpenAlex: W2113086962
Cited by: 368
References: 46
Citations by year: 2025: 1 · 2023: 3 · 2022: 2 · 2021: 1 · 2020: 2 · 2019: 3 · 2018: 4 · 2017: 3 · 2016: 5 · 2015: 8 · 2014: 4 · 2013: 11 · 2012: 3
FWCI: 18.34
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: American Lebanese Syrian Associated Charities
National Institutes of Health
National Cancer Institute (R01CA064140, P30CA021765)
Topics: Health Sciences › Medicine › Hematology › Acute Myeloid Leukemia Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: ETO, CBFβ, acute myeloid leukemia, transcriptional activation, alternative splicing, DNA-binding domain, nuclear localization, chromosomal translocation
MeSH terms: RUNX1 Translocation Partner 1 Protein, Amino Acid Sequence, Base Sequence, Cell Compartmentation, Cell Nucleus, Cloning, Molecular, DNA-Binding Proteins, Enhancer Elements, Genetic, Gene Expression Regulation, Molecular Sequence Data, Neoplasm Proteins, Protein Binding, Proto-Oncogene Proteins, Recombinant Fusion Proteins, Transcription Factors, Transcription, Genetic, Leukemia, Myeloid, Acute, Transcriptional Activation, Consensus Sequence, Alternative Splicing, DNA, Complementary, Core Binding Factors, Core Binding Factor Alpha 2 Subunit

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The t(8;21) Fusion Protein Interferes with AML-1B-Dependent Transcriptional Activation

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