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Direct inhibition of the NOTCH transcription factor complex
Open accessAbstract
Direct inhibition of transcription factor complexes remains a central challenge in the discipline of ligand discovery. In general, these proteins lack surface involutions suitable for high-affinity binding by small molecules. Here we report the design of synthetic, cell-permeable, stabilized alpha-helical peptides that target a critical protein-protein interface in the NOTCH transactivation complex. We demonstrate that direct, high-affinity binding of the hydrocarbon-stapled peptide SAHM1 prevents assembly of the active transcriptional complex. Inappropriate NOTCH activation is directly implicated in the pathogenesis of several disease states, including T-cell acute lymphoblastic leukaemia (T-ALL). The treatment of leukaemic cells with SAHM1 results in genome-wide suppression of NOTCH-activated genes. Direct antagonism of the NOTCH transcriptional program causes potent, NOTCH-specific anti-proliferative effects in cultured cells and in a mouse model of NOTCH1-driven T-ALL.
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Subramanian, A., Tamayo, P., Mootha, V. K., Mukherjee, S., Ebert, B. L., Gillette, M. A., Paulovich, A., Pomeroy, S. L., Golub, T. R., Lander, E. S., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506580102 · Cited by 53,625
Notch Signaling: Cell Fate Control and Signal Integration in Development
Artavanis-Tsakonas, S., Rand, M. D., & Lake, R. J. (1999) · Science · doi:10.1126/science.284.5415.770 · Cited by 5,909
Lamb, J., Crawford, E. D., Peck, D., Modell, J. W., Blat, I. C., Wrobel, M. J., Lerner, J., Brunet, J.-P., Subramanian, A., Ross, K. N., et al. (2006) · Science · doi:10.1126/science.1132939 · Cited by 5,257
Activating Mutations of NOTCH1 in Human T Cell Acute Lymphoblastic Leukemia
Weng, A. P., Ferrando, A. A., Lee, W., Morris, J. P., Silverman, L. B., Sanchez-Irizarry, C., Blacklow, S. C., Look, A. T., & Aster, J. C. (2004) · Science · doi:10.1126/science.1102160 · Cited by 2,706
Self-citationNotch signalling: a simple pathway becomes complex
Bray, S. J. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2009 · Cited by 2,620
A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain
De Strooper, B., Annaert, W., Cupers, P., Saftig, P., Craessaerts, K., Mumm, J. S., Schroeter, E. H., Schrijvers, V., Wolfe, M. S., Ray, W. J., et al. (1999) · Nature · doi:10.1038/19083 · Cited by 2,100
Determination of the helix and β form of proteins in aqueous solution by circular dichroism
Chen, Y.-H., Yang, J. T., & Chau, K. H. (1974) · Biochemistry · doi:10.1021/bi00713a027 · Cited by 2,070
Notch3 mutations in CADASIL, a hereditary adult-onset condition causing stroke and dementia
Joutel, A., Corpechot, C., Ducros, A., Vahedi, K., Chabriat, H., Mouton, P., Alamowitch, S., Domenga, V., Cécillion, M., Maréchal, E., et al. (1996) · Nature · doi:10.1038/383707a0 · Cited by 2,068
Ellisen, L. W., Bird, J., West, D. C., Soreng, A. L., Reynolds, T. C., Smith, S. D., & Sklar, J. (1991) · Cell · doi:10.1016/0092-8674(91)90111-b · Cited by 1,691
Mutations in NOTCH1 cause aortic valve disease
Garg, V., Muth, A. N., Ransom, J. F., Schluterman, M. K., Barnes, R., King, I. N., Grossfeld, P. D., & Srivastava, D. (2005) · Nature · doi:10.1038/nature03940 · Cited by 1,509
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CANALIS, E. M. (2018) · Osteoporosis International · doi:10.1007/s00198-018-4694-3 · Cited by 84
Helix-mediated protein–protein interactions as targets for intervention using foldamers
Edwards, T. A., & Wilson, A. J. (2011) · Amino Acids · doi:10.1007/s00726-011-0880-8 · Cited by 88
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Yu, J., & CANALIS, E. M. (2020) · Bone · doi:10.1016/j.bone.2020.115474 · Cited by 83
Notch-mediated patterning and cell fate allocation of pancreatic progenitor cells
Afelik, S., Qu, X., Hasrouni, E., Bukys, M. A., Deering, T. G., Nieuwoudt, S., Rogers, W., MacDonald, R. J., & Jensen, J. N. (2012) · Development · doi:10.1242/dev.075804 · Cited by 79
Breast Cancer Stem Cells: Something Out of Notching?
Harrison, H., Farnie, G., Brennan, K. R., & Clarke, R. B. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-1559 · Cited by 78
Peptidomimetics: A Synthetic Tool for Inhibiting Protein–Protein Interactions in Cancer
Mabonga, L., & Kappo, A. P. (2019) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-019-09831-5 · Cited by 81
Targeting BIG3–PHB2 interaction to overcome tamoxifen resistance in breast cancer cells
Yoshimaru, T., Komatsu, M., Matsuo, T., Chen, Y., Murakami, Y., Mizuguchi, K., Mizohata, E., Tsuyoshi Inoue, A., Akiyama, M. O., Yamaguchi, R., et al. (2013) · Nature Communications · doi:10.1038/ncomms3443 · Cited by 78
Sakamoto, K., Fujii, T., Kawachi, H., Miki, Y., Omura, K., Morita, K.-I., Kayamori, K., Katsube, K., & Yamaguchi, A. (2012) · Laboratory Investigation · doi:10.1038/labinvest.2012.9 · Cited by 78
Astudillo, L., Silva, T. G. D., Wang, Z., Han, X., Jin, K., VanWye, J., Zhu, X., Weaver, K. L., Oashi, T., Lopes, P. E. M., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-0061 · Cited by 78
PI3K/mTOR inhibition upregulates NOTCH-MYC signalling leading to an impaired cytotoxic response
Shepherd, C., Banerjee, L., Cheung, C. W., Mansour, M. R., Jenkinson, S., Gale, R. E., & Khwaja, A. (2012) · Leukemia · doi:10.1038/leu.2012.285 · Cited by 76
Blackburn, J. S., Liu, S., Raiser, D. M., Martinez, S. A., Feng, H., Meeker, N. D., Gentry, J., Neuberg, D. S., Look, A. T., Ramaswamy, S., et al. (2012) · Leukemia · doi:10.1038/leu.2012.116 · Cited by 75
Drug‐Like Properties in Macrocycles above MW 1000: Backbone Rigidity versus Side‐Chain Lipophilicity
Furukawa, A., Schwochert, J., Pye, C. R., Asano, D., Edmondson, Q. D., Turmon, A. C., Klein, V. G., Ono, S., Okada, O., & Lokey, R. S. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202004550 · Cited by 79
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Xu, W., Lau, Y. H., Fischer, G. W., Tan, Y. S., Chattopadhyay, A., de la Roche, M., Hyvönen, M., Verma, C. S., Spring, D. R., & Itzhaki, L. S. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.6b10234 · Cited by 75
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Bongiovanni, D., Saccomani, V., & Piovan, E. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091904 · Cited by 78
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Heitzler, P. (2010) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(10)92014-0 · Cited by 78
Fixierung cyclischer Peptide: Mimetika von Proteinstrukturmotiven
Hill, T. A., Shepherd, N. E., Diness, F., & Fairlie, D. P. (2014) · Angewandte Chemie · doi:10.1002/ange.201401058 · Cited by 72
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Gu, Y., Masiero, M., & Banham, A. H. (2016) · Oncotarget · doi:10.18632/oncotarget.7772 · Cited by 75
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Oyama, T., Harigaya, K., Sasaki, N., Okamura, Y., Kokubo, H., Saga, Y., Hozumi, K., Suganami, A., Tamura, Y., Nagase, T., et al. (2011) · Development · doi:10.1242/dev.062802 · Cited by 74
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Yu, L., Fang, F., Dai, X. J., Xu, H., Qi, X., Fang, M., & Xu, Y. (2017) · Scientific Reports · doi:10.1038/s41598-017-00301-w · Cited by 71
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Li, X., Tolbert, W. D., Hu, H., Gohain, N., Zou, Y., Niu, F., He, W., Yuan, W., Su, J., Pazgier, M., et al. (2018) · Chemical Science · doi:10.1039/c8sc03275k · Cited by 73
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Verdine, G. L., & Hilinski, G. J. (2012) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2012.01.004 · Cited by 70
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Firestone, A. J., & Chen, J. (2009) · ACS Chemical Biology · doi:10.1021/cb900249y · Cited by 71
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Kumar, M., Gupta, D., Singh, G., Sharma, S., Bhat, M., Prashant, C. K., Dinda, A. K., Kharbanda, S. M., Kufe, D. W., & Singh, H. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-2015 · Cited by 67
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Xie, Q., Wu, Q., Kim, L. J. Y., Miller, T. E., Liau, B. B., Mack, S. C., Yang, K., Factor, D. C., Fang, X., Huang, Z., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci86114 · Cited by 67
Gao, C., Dimitrov, T., Yong, K. J., Tatetsu, H., Jeong, H.-W., Luo, H. R., Bradner, J. E., Tenen, D. G., & Chai, L. (2013) · Blood · doi:10.1182/blood-2012-04-424275 · Cited by 65
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Liu, K., Xie, F., Zhao, T., Zhang, R., Gao, A., Chen, Y., Li, H., Zhang, S., Xiao, Z., Li, J., et al. (2020) · Molecular Therapy · doi:10.1016/j.ymthe.2020.01.012 · Cited by 54
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Metadata
- Authors
- Moellering, R. E., Cornejo, M., Davis, T. N., Bianco, C. D., Aster, J. C., Blacklow, S. C., Kung, A. L., Gilliland, D. G., Verdine, G. L., & Bradner, J. E.
- Affiliations
- Broad Institute (US)
- Brigham and Women's Hospital (US)
- Dana-Farber Cancer Institute (US)
- Harvard University (US)
- Corresponding author
- Verdine, Gregory L.
- Bradner, James E.
- ORCID
- Venue
- Nature
- Published
- 2009-11-12
- Volume
- 462
- Issue
- 7270
- Pages
- 182-188
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC2951323
- OpenAlex
- W2085948054
- Cited by
- 752
- References
- 51
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 12 · 2023: 30 · 2022: 21 · 2021: 28 · 2020: 43 · 2019: 35 · 2018: 47 · 2017: 43 · 2016: 34 · 2015: 56 · 2014: 70 · 2013: 76 · 2012: 75
- FWCI
- 32.31
- Type
- journal article
- Language
- en
- Update notices
- erratum (2010-01-21)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Iris (University of Trento) (submittedVersion)
- Funders
- National Institutes of Health (n01co12400-79-0-22, 5t32gm007598-41)
- National Cancer Institute (N01CO12400, N01-CO-012400, P01CA119070, R01CA092433, R56CA092433)
- National Institute of General Medical Sciences (5T32GM007598, T32-GM007598)
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- Notch signaling, hydrocarbon-stapled peptides, protein-protein interaction inhibition, T-cell acute lymphoblastic leukemia, Notch1, transcription factor antagonism, cell-permeable peptide
- MeSH terms
- Animals, Binding, Competitive, Cell Membrane Permeability, Disease Models, Animal, DNA-Binding Proteins, Humans, Models, Molecular, Nuclear Proteins, Peptides, Protein Binding, Substrate Specificity, Transcription Factors, Signal Transduction, Transcriptional Activation, Gene Expression Regulation, Neoplastic, Genome, Protein Structure, Secondary, Protein Structure, Tertiary, Drosophila Proteins, Cell Line, Tumor, Cell Proliferation, Mice, Immunoglobulin J Recombination Signal Sequence-Binding Protein, Receptor, Notch1, Precursor T-Cell Lymphoblastic Leukemia-Lymphoma
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