Transcriptomic and genomic studies classify NKL54 as a histone deacetylase inhibitor with indirect influence on MEF2-dependent transcription
Open accessAbstract
In leiomyosarcoma class IIa HDACs (histone deacetylases) bind MEF2 and convert these transcription factors into repressors to sustain proliferation. Disruption of this complex with small molecules should antagonize cancer growth. NKL54, a PAOA (pimeloylanilide o-aminoanilide) derivative, binds a hydrophobic groove of MEF2, which is used as a docking site by class IIa HDACs. However, NKL54 could also act as HDAC inhibitor (HDACI). Therefore, it is unclear which activity is predominant. Here, we show that NKL54 and similar derivatives are unable to release MEF2 from binding to class IIa HDACs. Comparative transcriptomic analysis classifies these molecules as HDACIs strongly related to SAHA/vorinostat. Low expressed genes are upregulated by HDACIs, while abundant genes are repressed. This transcriptional resetting correlates with a reorganization of H3K27 acetylation around the transcription start site (TSS). Among the upregulated genes there are several BH3-only family members, thus explaining the induction of apoptosis. Moreover, NKL54 triggers the upregulation of MEF2 and the downregulation of class IIa HDACs. NKL54 also increases the binding of MEF2D to promoters of genes that are upregulated after treatment. In summary, although NKL54 cannot outcompete MEF2 from binding to class IIa HDACs, it supports MEF2-dependent transcription through several actions, including potentiation of chromatin binding.
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This interplay is also engaged as an adaptive response to pan-HDACIs.
“An interplay that is also engaged as adaptive response to pan-HDACIs (Minisini et al., 2022).”
From HDACs and the epigenetic plasticity of cancer cells: target the complexity (2022) · cites this paper as Minisini et al., 2022
Upregulation of PD-L1 is a common feature of the response to HDACIs.
“More generally, upregulation of PD-L1 is a common feature of the response to HDACIs (Minisini et al., 2022).”
From HDACs and the epigenetic plasticity of cancer cells: target the complexity (2022) · cites this paper as Minisini et al., 2022
HDAC7 levels are downregulated after treatment with pan-HDACIs.
“Interestingly, HDAC7 levels are downregulated after treatment with pan-HDACIs (Minisini et al., 2022;Witt et al., 2017).”
From HDACs and the epigenetic plasticity of cancer cells: target the complexity (2022) · cites this paper as Minisini et al., 2022
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Love, M. I., Huber, W., & Anders, S. (2014) · Genome Biology · doi:10.1186/s13059-014-0550-8 · Cited by 95,106 · see citing works
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works
clusterProfiler: an R Package for Comparing Biological Themes Among Gene Clusters
Yu, G., Wang, L.-G., Han, Y., & He, Q.-Y. (2012) · OMICS: A Journal of Integrative Biology · doi:10.1089/omi.2011.0118 · Cited by 36,259 · see citing works
Salmon provides fast and bias-aware quantification of transcript expression
Patro, R., Duggal, G., Love, M. I., Irizarry, R. A., & Kingsford, C. (2017) · Nature Methods · doi:10.1038/nmeth.4197 · Cited by 12,700 · see citing works
ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB
Maier, J., Martinez, C., Kasavajhala, K., Wickstrom, L., Hauser, K., & Simmerling, C. L. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b00255 · Cited by 10,971 · see citing works
MultiQC: summarize analysis results for multiple tools and samples in a single report
Ewels, P., Magnusson, M., Lundin, S., & Käller, M. (2016) · Bioinformatics · doi:10.1093/bioinformatics/btw354 · Cited by 10,143 · see citing works
ReactomePA: an R/Bioconductor package for reactome pathway analysis and visualization
Yu, G., & He, Q. (2015) · Molecular BioSystems · doi:10.1039/c5mb00663e · Cited by 1,941 · see citing works
Morgan, H. L. (1965) · Journal of Chemical Documentation · doi:10.1021/c160017a018 · Cited by 1,716 · see citing works
Empirical Scoring Functions for Advanced Protein−Ligand Docking with PLANTS
Korb, O., Stützle, T., & Exner, T. E. (2009) · Journal of Chemical Information and Modeling · doi:10.1021/ci800298z · Cited by 1,358 · see citing works
Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors
Thome, M., Schneider, P., Hofmann, K., Fickenscher, H., Meinl, E., Neipel, F., Mattmann, C., Burns, K., Bodmer, J.-L., Schröter, M., et al. (1997) · Nature · doi:10.1038/386517a0 · Cited by 1,316 · see citing works
Measuring reproducibility of high-throughput experiments
Li, Q., Brown, J. B., Huang, H., & Bickel, P. J. (2010) · UC Berkeley · Cited by 915 · see citing works
BCL-2 family isoforms in apoptosis and cancer
Warren, C., Wong‐Brown, M. W., & Bowden, N. A. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1407-6 · Cited by 697 · see citing works
Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases
Lahm, A., Paolini, C., Pallaoro, M., Nardi, M. C., Jones, P., Neddermann, P., Sambucini, S., Bottomley, M. J., Lo Surdo, P., Carfı́, A., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706487104 · Cited by 566 · see citing works
Vinardo: A Scoring Function Based on Autodock Vina Improves Scoring, Docking, and Virtual Screening
Quiroga, R., & Villarreal, M. A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0155183 · Cited by 405 · see citing works
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Lobera, M., Madauss, K. P., Pohlhaus, D. T., Wright, Q. G., Trocha, M., Schmidt, D. R., Baloglu, E., Trump, R. P., Head, M. S., Hofmann, G. A., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1223 · Cited by 384 · see citing works
Tximeta: Reference sequence checksums for provenance identification in RNA-seq
Love, M. I., Soneson, C., Hickey, P. F., Johnson, L. K., Pierce‐Ward, N. T., Shepherd, L. A., Morgan, M. T., & Patro, R. (2020) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1007664 · Cited by 360 · see citing works
Bottomley, M. J., Surdo, P. L., Giovine, P. D., Cirillo, A., Scarpelli, R., Ferrigno, F., JONES, P. G., Neddermann, P., Francesco, R. D., Steinkühler, C., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803514200 · Cited by 319 · see citing works
Pimelic Diphenylamide 106 Is a Slow, Tight-binding Inhibitor of Class I Histone Deacetylases
Chou, C. J., Herman, D., & Gottesfeld, J. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807045200 · Cited by 223 · see citing works
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Grégoire, S., Xiao, L., Nie, J., Zhang, X., Xu, M., Li, J., Wong, J., Seto, E., & Yang, X.-J. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00882-06 · Cited by 203 · see citing works
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Bolden, J. E., Shi, W., Jankowski, K., Kan, C.-Y., Cluse, L. A., Martin, B. P., MacKenzie, K. L., Smyth, G. K., & Johnstone, R. W. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.9 · Cited by 197 · see citing works
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Pon, J., & Marra, M. (2015) · OncoTarget · doi:10.18632/oncotarget.6223 · Cited by 182 · see citing works
Qu, K., Zaba, L. C., Satpathy, A. T., Giresi, P. G., Li, R., Jin, Y., Armstrong, R. J., Chen, J., Schmitt, N., Rahbar, Z., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.05.008 · Cited by 178 · see citing works
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Greer, C. B., Tanaka, Y., Kim, Y. J., Xie, P., Zhang, M. Q., Park, I.-H., & Kim, T. H. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.10.013 · Cited by 174 · see citing works
Witt, A. E., Lee, C.-W., Lee, T. I., Azzam, D. J., Wang, B., Caslini, C., Petrocca, F., Grosso, J., Jones, M., Cohick, E. B., et al. (2017) · Oncogene · doi:10.1038/onc.2016.337 · Cited by 172 · see citing works
Ma, K., Chan, J. K. L., Zhu, G., & Wu, Z. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.9.3575-3582.2005 · Cited by 165 · see citing works
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Gryder, B. E., Pomella, S., Sayers, C. M., Wu, X., Song, Y., Chiarella, A. M., Bagchi, S., Chou, H.-C., Sinniah, R., Walton, A., et al. (2019) · Nature Genetics · doi:10.1038/s41588-019-0534-4 · Cited by 162 · see citing works
Paroni, G., Mizzau, M., Henderson, C. J., Sal, G. D., Schneider, C., & Brancolini, C. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-08-0624 · Cited by 149 · see citing works
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Han, A., Pan, F., Stroud, J. C., Youn, H., Liu, J. O., & Chen, L. (2003) · Nature · doi:10.1038/nature01555 · Cited by 127 · see citing works
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Giorgio, E. D., & Brancolini, C. (2016) · Epigenomics · doi:10.2217/epi.15.106 · Cited by 124 · see citing works
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Han, A., He, J., Wu, Y., Liu, J. O., & Chen, L. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.033 · Cited by 107 · see citing works
Perkel, J. M. (2015) · Nature · doi:10.1038/518125a · Cited by 104 · see citing works
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Fischer, G., Rossmann, M., & Hyvönen, M. (2015) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2015.04.006 · Cited by 97 · see citing works
Kim, Y. J., Greer, C. B., Cecchini, K. R., Harris, L. N., Tuck, D. P., & Kim, T. H. (2013) · Oncogene · doi:10.1038/onc.2013.32 · Cited by 95 · see citing works
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Rafehi, H., Balcerczyk, A., Lunke, S., Kaspi, A., Ziemann, M., Kurup, H. K. N., Okabe, J., Khurana, I., Ooi, J. Y. Y., Khan, A. W., et al. (2014) · Genome Research · doi:10.1101/gr.168781.113 · Cited by 94 · see citing works
Sanchez, G. J., Richmond, P. A., Bunker, E. N., Karman, S. S., Azofeifa, J. G., Garnett, A. T., Xu, Q., Wheeler, G. E., Toomey, C. M., Zhang, Q., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1225 · Cited by 92 · see citing works
Emerging roles for MEF2 in brain development and mental disorders
Assali, A., Harrington, A. J., & Cowan, C. W. (2019) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2019.04.008 · Cited by 92 · see citing works
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Ragno, R., Frasca, S., Manetti, F., Brizzi, A., & Massa, S. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0493921 · Cited by 70 · see citing works
Self-citationMuscat, A. M., Popovski, D., Jayasekara, W. S. N., Rossello, F. J., Ferguson, M., Marini, K. D., Alamgeer, M., Algar, E. M., Downie, P., Watkins, D. N., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-2260 · Cited by 70 · see citing works
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Self-citationGiorgio, E. D., Paluvai, H., Dalla, E., Ranzino, L., Renzini, A., Moresi, V., Minisini, M., Picco, R., & Brancolini, C. (2021) · Genome biology · doi:10.1186/s13059-021-02340-z · Cited by 67 · see citing works
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Brown, J. A. L., Bourke, E., Eriksson, L. A., & Kerin, M. J. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160081 · Cited by 63 · see citing works
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He, J., Ye, J., Cai, Y., Riquelme, C. A., Liu, J. O., Liu, X., Han, A., & Chen, L. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr030 · Cited by 62 · see citing works
Ragno, R. (2019) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-019-00231-x · Cited by 59 · see citing works
Self-citationGiorgio, E. D., Gagliostro, E., Clocchiatti, A., & Brancolini, C. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.01461-14 · Cited by 58 · see citing works
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Giorgio, E. D., Gagliostro, E., & Brancolini, C. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1727-8 · Cited by 57 · see citing works
Self-citationMusmuca, I., Caroli, A., Mai, A., Kaushik‐Basu, N., Arora, P., & Ragno, R. (2010) · Journal of Chemical Information and Modeling · doi:10.1021/ci9004749 · Cited by 57 · see citing works
Self-citationGiorgio, E. D., Dalla, E., Franforte, E., Paluvai, H., Minisini, M., Trevisanut, M., Picco, R., & Brancolini, C. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1120 · Cited by 57 · see citing works
Self-citationGiorgio, E. D., Franforte, E., Cefalù, S., Rossi, S., Tos, A. P. D., Brenca, M., Polano, M., Maestro, R., Paluvai, H., Picco, R., et al. (2017) · PLoS Genetics · doi:10.1371/journal.pgen.1006752 · Cited by 56 · see citing works
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Jayathilaka, N., Han, A., Gaffney, K. J., Dey, R., Jarusiewicz, J., Noridomi, K., Philips, M. A., Lei, X., He, J., Ye, J., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks189 · Cited by 54 · see citing works
Halsall, J. A., Turan, N., Wiersma, M., & Turner, B. M. (2015) · Epigenetics & Chromatin · doi:10.1186/s13072-015-0021-9 · Cited by 50 · see citing works
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Self-citationSavickienė, J., Borutinskaite, V. V., Treigytė, G., et al. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.08.010 · Cited by 44 · see citing works
Cutano, V., Di Giorgio, E., Minisini, M., Picco, R., Dalla, E., & Brancolini, C. (2019) · Molecular Oncology · doi:10.1002/1878-0261.12503 · Cited by 44 · see citing works
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Cersosimo, U., Sgorbissa, A., Foti, C., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm501336h · Cited by 41 · see citing works
Clocchiatti, A., Giorgio, E. D., Ingrao, S., Meyer‐Almes, F., Tripodo, C., & Brancolini, C. (2012) · The FASEB Journal · doi:10.1096/fj.12-209346 · Cited by 40 · see citing works
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Angelelli, C., Magli, A., Ferrari, D., Ganassi, M., Matafora, V., Parise, F., Razzini, G., Bachi, A., Ferrari, S. M., & Molinari, S. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm1114 · Cited by 34 · see citing works
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Laszig, S., Boedicker, C., Weiser, T., Knapp, S., & Fulda, S. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.05.008 · Cited by 32 · see citing works
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Algar, S., Martín‐Martinez, M., & González‐Muñiz, R. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.113015 · Cited by 26 · see citing works
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Lamparter, C. L., & Winn, L. M. (2016) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2016.07.001 · Cited by 13 · see citing works
Vidal-Sancho, L., Fernández‐García, S., Solés-Tarrés, I., Alberch, J., & Xifró, X. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02041-x · Cited by 12 · see citing works
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Montella, L., Altucci, L., Sarno, F., Buonerba, C., SIMONE, S. D., Facchini, B. A., Franzese, E., Vita, F. D., Tafuto, S., Berretta, M., et al. (2021) · Cancers · doi:10.3390/cancers13102359 · Cited by 11 · see citing works
Iuliano, L., Drioli, S., Pignochino, Y., et al. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-20-0521 · Cited by 8 · see citing works
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- [24]Korb O., Stutzle T., Exner T.E. Plants: application of ant colony optimization to structure-based drug design. Ant colony optimization and swarm intelligence. Proc. AMIA Annu. Fall Symp. 2006; 4150: 247– 258.
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HDACs and the epigenetic plasticity of cancer cells: target the complexity
Brancolini, C., Gagliano, T., & Minisini, M. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108190 · Cited by 55 · see citing works
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- Authors
- Minisini, M., Di Giorgio, E., Kerschbamer, E., Dalla, E., Faggiani, M., Franforte, E., Meyer-Almes, F.-J., Ragno, R., Antonini, L., Mai, A., Fiorentino, F., Rotili, D., Chinellato, M., Perin, S., Cendron, L., Weichenberger, C. X., Angelini, A., & Brancolini, C.
- Affiliations
- University of Udine (IT)
- Department of Medicine, Università degli Studi di Udine. P.le Kolbe 4, 33100 Udine Italy
- Eurac Research (IT)
- Department of Chemical Engineering and Biotechnology, University of Applied Science, Haardtring 100, 64295 Darmstadt, Germany
- Sapienza University of Rome (IT)
- University of Padua (IT)
- Ca' Foscari University of Venice (IT)
- Corresponding author
- Brancolini, Claudio
- ORCID
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2022-02-12
- Volume
- 50
- Issue
- 5
- Pages
- 2566-2586
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC8934631
- OpenAlex
- W4210302835
- Cited by
- 28
- References
- 73
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 9 · 2023: 5 · 2022: 4
- FWCI
- 2.04
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Nucleic Acids Research (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Iris (Roma Tre University) (submittedVersion, cc-by)
- Institutional Research Information System (University of Udine) (submittedVersion, cc-by-nc-nd)
- Institutional Research Information System (University of Udine) (submittedVersion)
- IRIS Research product catalog (Sapienza University of Rome) (submittedVersion, other-oa)
- ARCA (Università Ca' Foscari Venezia) (submittedVersion, cc-by-nc-nd)
- Open Research (University of Surrey) (submittedVersion, other-oa)
- Padua Research Archive (University of Padova) (submittedVersion, cc-by)
- Funders
- PRIN (2017JL8SRX)
- Interreg Italia-Osterreich (ITAT1054 EPIC)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- histone deacetylase inhibitors, class IIa HDACs, MEF2, MEF2D, vorinostat, H3K27 acetylation, transcriptional reprogramming, apoptosis, leiomyosarcoma, chromatin binding
- MeSH terms
- Vorinostat, Acetylation, Histone Deacetylases, Histone Deacetylase Inhibitors, Transcriptome, MEF2 Transcription Factors
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