Targeting HDAC3, a new partner protein of AKT in the reversal of chemoresistance in acute myeloid leukemia via DNA damage response

Long, J; Fang, W Y; Chang, L; Gao, W H; Shen, Y; Jia, M Y; Zhang, Y X; Wang, Y; Dou, H B; Zhang, W J; Zhu, J; Liang, A B; Li, J M; Hu, Jiong

doi:10.1038/leu.2017.130

Cited by 83Histone Deacetylase Inhibitors ResearchAcute Myeloid Leukemia ResearchEpigenetics and DNA Methylation

Targeting HDAC3, a new partner protein of AKT in the reversal of chemoresistance in acute myeloid leukemia via DNA damage response

Long, J, Fang, W Y, Chang, L, Gao, W H, Shen, Y, Jia, M Y, Zhang, Y X, Wang, Y +6 more·2017·Leukemia

DOI 10.1038/leu.2017.130

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Abstract

Resistance to cytotoxic chemotherapy drugs remains as the major cause of treatment failure in acute myeloid leukemia. Histone deacetylases (HDAC) are important regulators to maintain chromatin structure and control DNA damage; nevertheless, how each HDAC regulates genome stability remains unclear, especially under genome stress conditions. Here, we identified a mechanism by which HDAC3 regulates DNA damage repair and mediates resistance to chemotherapy drugs. In addition to inducing DNA damage, chemotherapy drugs trigger upregulation of HDAC3 expression in leukemia cells. Using genetic and pharmacological approaches, we show that HDAC3 contributes to chemotherapy resistance by regulating the activation of AKT, a well-documented factor in drug resistance development. HDAC3 binds to AKT and deacetylates it at the site Lys20, thereby promoting the phosphorylation of AKT. Chemotherapy drug exposure enhances the interaction between HDAC3 and AKT, resulting in decrease in AKT acetylation and increase in AKT phosphorylation. Whereas HDAC3 depletion or inhibition abrogates these responses and meanwhile sensitizes leukemia cells to chemotoxicity-induced apoptosis. Importantly, in vivo HDAC3 suppression reduces leukemia progression and sensitizes MLL-AF9+ leukemia to chemotherapy. Our findings suggest that combination therapy with HDAC3 inhibitor and genotoxic agents may constitute a successful strategy for overcoming chemotherapy resistance.

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HDAC3 deacetylates lysine 14 and 20 of Akt.
“HDAC3 deacetylates lysine 14 and 20 of Akt (Long et al., 2017;Yan et al., 2018).”
From HDACs and the epigenetic plasticity of cancer cells: target the complexity (2022) · cites this paper as Long et al., 2017
Akt1 is another non-histone target of HDAC3-mediated deacetylation.
“Akt1 is another non-histone target of HDAC3 mediated deacetylation (Long et al., 2017;Yan et al., 2018).”
From HDACs and the epigenetic plasticity of cancer cells: target the complexity (2022) · cites this paper as Long et al., 2017

Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040 · see citing works
Acute Myeloid Leukemia
Döhner, H., Weisdorf, D. J., & Bloomfield, C. D. (2015) · New England Journal of Medicine · doi:10.1056/nejmra1406184 · Cited by 3,354 · see citing works
New and emerging HDAC inhibitors for cancer treatment
West, A. C., & Johnstone, R. W. (2014) · Journal of Clinical Investigation · doi:10.1172/jci69738 · Cited by 1,404 · see citing works
MLL translocations, histone modifications and leukaemia stem-cell development
Krivtsov, A., & Armstrong, S. (2007) · Nature Reviews. Cancer · doi:10.1038/nrc2253 · Cited by 1,294 · see citing works
DNA damage and the balance between survival and death in cancer biology
Roos, W. P., Thomas, A. D., & Kaina, B. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2015.2 · Cited by 1,189 · see citing works
Lysine Acetylation: Codified Crosstalk with Other Posttranslational Modifications
Yang, X.-J., & Seto, E. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.002 · Cited by 1,006 · see citing works
Histone Deacetylase Inhibitors in Cancer Therapy
Lane, A. A., & Chabner, B. A. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2009.22.1291 · Cited by 880 · see citing works
Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining
Miller, K. M., Tjeertes, J. V., Coates, J., Legube, G., Polo, S. E., Britton, S., & Jackson, S. P. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1899 · Cited by 629 · see citing works
Therapeutic opportunities within the DNA damage response
Pearl, L. H., Schierz, A. C., Ward, S. E., Al-Lazikani, B., & Pearl, F. M. G. (2015) · Nature Reviews Cancer · doi:10.1038/nrc3891 · Cited by 587 · see citing works
Activation of the PI3K/Akt pathway and chemotherapeutic resistance
West, K. A., Castillo, S. S., & Dennis, P. A. (2002) · Drug Resistance Updates · doi:10.1016/s1368-7646(02)00120-6 · Cited by 583 · see citing works
Acute myeloid leukaemia in adults
Ferrara, F., & Schiffer, C. A. (2013) · The Lancet · doi:10.1016/s0140-6736(12)61727-9 · Cited by 566 · see citing works
Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate
Watson, P. J., Fairall, L., Santos, G. M., & Schwabe, J. W. R. (2012) · Nature · doi:10.1038/nature10728 · Cited by 505 · see citing works
Survival of acute myeloid leukemia cells requires PI3 kinase activation
Xu, Q., Simpson, S.-E., Scialla, T. J., Bagg, A., & Carroll, M. P. (2003) · Blood · doi:10.1182/blood-2002-11-3429 · Cited by 469 · see citing works
PKBα/Akt1 Acts Downstream of DNA-PK in the DNA Double-Strand Break Response and Promotes Survival
Bozulic, L., Sürücü, B., Hynx, D., & Hemmings, B. A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.024 · Cited by 386 · see citing works
Deletion of Histone Deacetylase 3 Reveals Critical Roles in S Phase Progression and DNA Damage Control
Bhaskara, S., Chyla, B., Amann, J. M., Knutson, S. K., Cortez, D., Sun, Z., & Hiebert, S. W. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.030 · Cited by 369 · see citing works
Hdac3 is essential for the maintenance of chromatin structure and genome stability
Bhaskara, S., Knutson, S. K., Jiang, G., Chandrasekharan, M. B., Wilson, A. J., Zheng, S., Yenamandra, A., Locke, K., Yuan, J.-L., Bonine-Summers, A. R., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.10.022 · Cited by 353 · see citing works
The Deacetylase SIRT1 Promotes Membrane Localization and Activation of Akt and PDK1 During Tumorigenesis and Cardiac Hypertrophy
Sundaresan, N. R., Pillai, V. B., Wolfgeher, D., Samant, S. A., Vasudevan, P., Parekh, V., Raghuraman, H., Cunningham, J. M., Gupta, M., & Gupta, M. P. (2011) · Science Signaling · doi:10.1126/scisignal.2001465 · Cited by 345 · see citing works
Akt: A Double-Edged Sword in Cell Proliferation and Genome Stability
Xu, N., Lao, Y., Zhang, Y., & Gillespie, D. A. (2012) · Journal of Oncology · doi:10.1155/2012/951724 · Cited by 308 · see citing works
PLECKSTRIN HOMOLOGY DOMAINS: A Common Fold with Diverse Functions
Rebecchi, M. J., & Scarlata, S. (1998) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.27.1.503 · Cited by 291 · see citing works
PI3-kinase/Akt is constitutively active in primary acute myeloid leukaemia cells and regulates survival and chemoresistance via NF-kB, MAPkinase and p53 pathways
Grandage, V., Gale, R. E., Linch, D. C., & Khwaja, A. (2005) · Leukemia · doi:10.1038/sj.leu.2403653 · Cited by 282 · see citing works
A phosphorylation-acetylation switch regulates STAT1 signalingPreprint
Krämer, O. H., Knauer, S. K., Greiner, G., Jandt, E., Reichardt, S., Gührs, K., Stauber, R. H., Böhmer, F., & Heinzel, T. (2009) · Genes & Development · doi:10.1101/gad.479209 · Cited by 282 · see citing works
Mouse models of human AML accurately predict chemotherapy responsePreprint
Zuber, J. A., Radtke, I., Pardee, T. S., Zhao, Z., Rappaport, A., Luo, W., McCurrach, M. E., Yang, M., Dolan, M. E., Kogan, S. C., et al. (2009) · Genes & Development · doi:10.1101/gad.1771409 · Cited by 279 · see citing works
Acetylation site specificities of lysine deacetylase inhibitors in human cells
Schölz, C., Weinert, B. T., Wagner, S., Beli, P., Miyake, Y., Qi, J., Jensen, L. J., Streicher, W. W., McCarthy, A. R., Westwood, N. J., et al. (2015) · Nature Biotechnology · doi:10.1038/nbt.3130 · Cited by 271 · see citing works
Differential expression of histone deacetylases HDAC1, 2 and 3 in human breast cancer - overexpression of HDAC2 and HDAC3 is associated with clinicopathological indicators of disease progression
Müller, B. M., Jana, L., Kasajima, A., Lehmann, A., Prinzler, J., Budczies, J., Winzer, K., Dietel, M., Weichert, W., & Denkert, C. (2013) · BMC Cancer · doi:10.1186/1471-2407-13-215 · Cited by 258 · see citing works
Constitutive phosphorylation of Akt/PKB protein in acute myeloid leukemia: its significance as a prognostic variable
Min, Y. H., Eom, J., Cheong, J., Maeng, H. M., Kim, J. Y., Jeung, H.-K., Lee, S. T., Lee, M., Hahn, J. S., & Ko, Y. (2003) · Leukemia · doi:10.1038/sj.leu.2402874 · Cited by 238 · see citing works
research paper: Differential expression of <i>HDAC3, HDAC7</i> and <i>HDAC9</i> is associated with prognosis and survival in childhood acute lymphoblastic leukaemia
Moreno, D. A., Scrideli, C. A., Cortez, M. A. A., De Paula Queiroz, R., Valera, E. T., Da Silva Silveira, V., Yunes, J. A., Brandalise, S. R., & Tone, L. G. (2010) · British Journal of Haematology · doi:10.1111/j.1365-2141.2010.08301.x · Cited by 208 · see citing works
Targeting of AKT1 enhances radiation toxicity of human tumor cells by inhibiting DNA-PKcs-dependent DNA double-strand break repair
Toulany, M., Kehlbach, R., Florczak, U., Sak, A., Wang, S., Chen, J., Löbrich, M., & Rodemann, H. P. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-2200 · Cited by 186 · see citing works
Histone deacetylase inhibitors as radiosensitisers: effects on DNA damage signalling and repair
Grošelj, B., Sharma, N. L., Hamdy, F. C., Kerr, M., & Kiltie, A. E. (2013) · British Journal of Cancer · doi:10.1038/bjc.2013.21 · Cited by 185 · see citing works
Akt Promotes Post-Irradiation Survival of Human Tumor Cells through Initiation, Progression, and Termination of DNA-PKcs–Dependent DNA Double-Strand Break Repair
Toulany, M., Lee, K. J., Fattah, K. R., Lin, Y., Fehrenbacher, B., Schaller, M., Chen, B. P., Chen, D. J., & Rodemann, H. P. (2012) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-11-0592 · Cited by 183 · see citing works
Dysregulated Class I histone deacetylases are indicators of poor prognosis in multiple myeloma
Mithraprabhu, S., Kalff, A., Chow, A. L., Khong, T. T., & Spencer, A. G. (2014) · Epigenetics · doi:10.4161/15592294.2014.983367 · Cited by 176 · see citing works
Inhibition of histone deacetylase overcomes rapamycin-mediated resistance in diffuse large B-cell lymphoma by inhibiting Akt signaling through mTORC2
Gupta, M., Ansell, S. M., Novak, A. J., Kumar, S. K., Kaufmann, S. H., & Witzig, T. E. (2009) · Blood · doi:10.1182/blood-2009-05-220889 · Cited by 163 · see citing works
Histone deacetylase 3 as a novel therapeutic target in multiple myeloma
Minami, J., Suzuki, R., Mazitschek, R., Gorgun, G., Ghosh, B., Cirstea, D., Hu, Y., Mimura, N., Ohguchi, H., Cottini, F., et al. (2014) · Leukemia · doi:10.1038/leu.2013.231 · Cited by 159 · see citing works
Histone deacetylase inhibitors for the treatment of myelodysplastic syndrome and acute myeloid leukemia
Quintás‐Cardama, A., Santos, F. P. D. S., & Garcia‐Manero, G. (2010) · Leukemia · doi:10.1038/leu.2010.276 · Cited by 153 · see citing works
The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity
Liu, Y., Cheney, M. D., Gaudet, J., Chruszcz, M., Lukasik, S. M., Sugiyama, D., Lary, J. W., Cole, J. L., Dauter, Z., Minor, W., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.03.012 · Cited by 137 · see citing works
Regulation of STAT3 by histone deacetylase-3 in diffuse large B-cell lymphoma: implications for therapy
Gupta, M., Han, J. J., Stenson, M. J., Wellik, L. E., & Witzig, T. E. (2011) · Leukemia · doi:10.1038/leu.2011.340 · Cited by 134 · see citing works
Histone deacetylase inhibitors and genomic instability
Éot-Houllier, G., Fulcrand, G., Magnaghi-Jaulin, L., & Jaulin, C. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.06.005 · Cited by 121 · see citing works
Mouse models of MLL leukemia: recapitulating the human disease.
Milne, T. (2017) · Blood · doi:10.1182/blood-2016-10-691428 · Cited by 95 · see citing works
Histone Deacetylase in Chronic Lymphocytic Leukemia
Wang, J. C., Kafeel, M. I., Avezbakiyev, B., Chen, C., Sun, Y., Rathnasabapathy, C., Kalavar, M. R., He, Z., Burton, J., & Lichter, S. (2011) · Oncology · doi:10.1159/000334577 · Cited by 92 · see citing works
Histone Deacetylase 3 Suppression Increases PH Domain and Leucine-rich Repeat Phosphatase (Phlpp)1 Expression in Chondrocytes to Suppress Akt Signaling and Matrix Secretion
Bradley, E. W., Shull, L. C., & Westendorf, J. J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.423723 · Cited by 91 · see citing works
Sensitisation of HL60 human leukaemic cells to cytotoxic drug-induced apoptosis by inhibition of PI3-kinase survival signals
O'Gorman, D., McKenna, S. L., McGahon, A. J., Knox, K., & Cotter, T. G. (2000) · Leukemia · doi:10.1038/sj.leu.2401726 · Cited by 81 · see citing works
Class I histone deacetylases 1, 2 and 3 are highly expressed in classical Hodgkin's lymphoma
Adams, H., Fritzsche, F. R., Dirnhofer, S., Kristiansen, G., & Tzankov, A. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728221003796609 · Cited by 78 · see citing works
PKB/Akt promotes DSB repair in cancer cells through upregulating Mre11 expression following ionizing radiation
Deng, R., Tang, J., Ma, J.-G., Chen, S.-P., Xia, L.-P., Zhou, W.-J., Li, D., Feng, G.-K., Zeng, Y.-X., & Zhu, X.-F. (2010) · Oncogene · doi:10.1038/onc.2010.467 · Cited by 75 · see citing works
Functional-genetic dissection of HDAC dependencies in mouse lymphoid and myeloid malignancies
Matthews, G. M., Mehdipour, P., Cluse, L. A., Falkenberg, K. J., Wang, E., Roth, M., Santoro, F., Vidacs, E., Stanley, K. L., House, C. M., et al. (2015) · Blood · doi:10.1182/blood-2015-03-632984 · Cited by 60 · see citing works
MERIT40 Is an Akt Substrate that Promotes Resolution of DNA Damage Induced by Chemotherapy
Brown, K., Montaser‐Kouhsari, L., Beck, A. H., & Toker, A. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.05.004 · Cited by 45 · see citing works
Multidrug resistance in leukemic cell line K562/A02 induced by doxorubicin.
Yang, C., Luan, F.-J., Xiong, D., Liu, B.-R., Xu, Y., & Gu, K.-S. (1995) · PubMed · Cited by 36 · see citing works
A phase I/II study of imatinib plus reinduction therapy for c-kit-positive relapsed/refractory acute myeloid leukemia: inhibition of Akt activation correlates with complete response
Brandwein, J. M., Hedley, D. W., Chow, S., Schimmer, A. D., Yee, K. W. L., Schuh, A. C., Gupta, V. K., Xu, W., Kamel‐Reid, S., & Minden, M. D. (2011) · Leukemia · doi:10.1038/leu.2011.34 · Cited by 35 · see citing works
Valproic Acid Ameliorates Graft-versus-Host Disease by Downregulating Th1 and Th17 Cells
Long, J., Li, C., Shen, Y., Gao, W.-H., Wu, Y., Dou, H.-B., Huang, M., Wang, Y., Fang, W., Shan, J., et al. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1500578 · Cited by 31 · see citing works
Histone deacetylase complexes as caretakers of genome stability
Lahue, R. S., & Frizzell, A. (2012) · Epigenetics · doi:10.4161/epi.20922 · Cited by 30 · see citing works
Inactivating mutation in histone deacetylase 3 stabilizes its active conformation
Arrar, M., de Oliveira, C. A. F., & McCammon, J. A. (2013) · Protein Science · doi:10.1002/pro.2317 · Cited by 11 · see citing works

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An, P., Chen, F., Li, Z., Ling, Y., Peng, Y., Zhang, H., Li, J., Chen, Z., & Wang, H. (2020) · Oncogene · doi:10.1038/s41388-020-1337-x · Cited by 67 · see citing works
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Yu, S., Zhu, K.-Y., Chen, J., Liu, X.-Z., Xu, P., Zhang, W., Li, Y., Guo, H., & Zhu, J. (2018) · Nature Communications · doi:10.1038/s41467-018-05548-z · Cited by 63 · see citing works
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Ye, J., Zha, J., Shi, Y., Li, Y., Yuan, D., Chen, Q., Lin, F., Fang, Z., Yu, Y., Dai, Y., et al. (2019) · Clinical Epigenetics · doi:10.1186/s13148-019-0723-0 · Cited by 61 · see citing works
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Yan, Y., An, J., Yang, Y., Wu, D., Bai, Y., Cao, W., Ma, L., Chen, J., Yu, Z., He, Y., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708478 · Cited by 53 · see citing works
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The nuclear receptor corepressor NCoR1 regulates hematopoiesis and leukemogenesis in vivo
Wan, X., Liu, L., Zhou, P., Hui, X., He, Q., Yu, F., Zhang, W., Ding, X., Yuan, X., Zhang, N., et al. (2019) · Blood Advances · doi:10.1182/bloodadvances.2018022756 · Cited by 21 · see citing works
Histone deacetylase 2 regulates the doxorubicin (Dox) resistance of hepatocarcinoma cells and transcription of ABCB1
Yang, Y., Zhang, J., Wu, T., Xu, X., Cao, G., Li, H., & Chen, X. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.11.043 · Cited by 19 · see citing works
Programmed cell death 5 suppresses AKT-mediated cytoprotection of endothelium
Lee, S., Seo, J., Park, S., Jeong, M., Choi, H.-K., Lee, C. J., Kim, M., Guk, G., Lee, S.-Y., Park, H., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1712918115 · Cited by 18 · see citing works
Selective Inhibition of HDAC Class I Sensitizes Leukemia and Neuroblastoma Cells to Anticancer Drugs
Vagapova, E. R., Kozlov, M. V., Lebedev, T. D., Ivanenko, K. A., Leonova, O. G., Попенко, В. И., Spirin, P., Kochetkov, S. N., & Prassolov, V. (2021) · Biomedicines · doi:10.3390/biomedicines9121846 · Cited by 17 · see citing works
Ubiquitin chromatin remodelling after DNA damage is associated with the expression of key cancer genes and pathways
Cole, A. J., Dickson, K.-A., Liddle, C., Stirzaker, C., Shah, J. S., Clifton-Bligh, R. J., & Marsh, D. J. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03552-5 · Cited by 17 · see citing works
HDAC1 regulates the chemosensitivity of laryngeal carcinoma cells via modulation of interleukin-8 expression
Ding, S., Tang, Z., Jiang, Y., Luo, P., Qing, B., Wei, Y., Zhang, S., & Tang, R. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.173923 · Cited by 14 · see citing works
Scutellarin circumvents chemoresistance, promotes apoptosis, and represses tumor growth by HDAC/miR-34a-mediated down-modulation of Akt/mTOR and NF-κB-orchestrated signaling pathways in multiple myeloma.
Li, L., Zheng, Y., Zhang, W., Hou, L., & Gao, Y. (2020) · PubMed Central · Cited by 12 · see citing works
High Histone Deacetylase 2/3 Expression in Non-Functioning Pituitary Tumors
Zhao, W., Jiang, X., Weisenthal, K., Ma, J., Botticelli, E. M., Zhou, Y., Hedley‐Whyte, E. T., Wang, B., Swearingen, B., Soberman, R. J., et al. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.875122 · Cited by 12 · see citing works
HDAC-driven mechanisms in anticancer resistance: epigenetics and beyond
Minisini, M., Mascaro, M., & Brancolini, C. (2024) · Cancer Drug Resistance · doi:10.20517/cdr.2024.103 · Cited by 11 · see citing works
Clinical outcome of FLAG-IDA chemotherapy sequential with Flu–Bu3 conditioning regimen in patients with refractory AML: a parallel study from Shanghai Institute of Hematology and Institut Paoli-Calmettes
Wang, X., Devillier, R., Wan, M., Decroocq, J., Tian, L., Fürst, S., Wang, L., Vey, N., Fan, X., Blaise, D., et al. (2018) · Bone Marrow Transplantation · doi:10.1038/s41409-018-0283-5 · Cited by 11 · see citing works
Discovery of Highly Potent and Orally Bioavailable Histone Deacetylase 3 Inhibitors as Immunomodulators and Enhancers of DNA-Damage Response in Cancer Therapy
Li, S., Hu, Z., Pan, W., Wu, H., Peng, W., Wu, Y., Jiang, F., & Peng, X. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02445 · Cited by 9 · see citing works
Acetylation stabilizes the signaling protein WISP2 by preventing its degradation to suppress the progression of acute myeloid leukemia
Zhang, H., Song, W., Ma, X., Yu, M., Chen, L., & Tao, Y. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.102971 · Cited by 9 · see citing works
Spatiotemporal 7q11.23 protein network analysis implicates the role of DNA repair pathway during human brain development
Chen, L., Wang, W., Cai, W., Song, W., Qian, W., & Lin, G. N. (2021) · Scientific Reports · doi:10.1038/s41598-021-87632-x · Cited by 9 · see citing works
[Harlequin syndrome (unilateral flushing and sweating attack) due to a spinal invasion of the left apical lung cancer].
Umeki, S., Tamai, H., Yagi, S., Soejima, R., & Higashi, Y. (1990) · PubMed · Cited by 9 · see citing works
HDAC11 mediates the ubiquitin-dependent degradation of p53 and inhibits the anti-leukemia effect of PD0166285
Zhou, Z., Zhong, L., Chu, X., Wan, P., Dan, W., Shao, X., Chen, S., Zhang, Z., Lu, Y., & Liu, B. (2023) · Medical Oncology · doi:10.1007/s12032-023-02196-2 · Cited by 8 · see citing works
Increased Susceptibility and Intrinsic Apoptotic Signaling in Neurons by Induced HDAC3 Expression
Schmitt, H. M., Fehrman, R. L., Maes, M. E., Yang, H. M., Guo, L., Schlamp, C. L., Pelzel, H. R., & Nickells, R. W. (2021) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.62.10.14 · Cited by 8 · see citing works
HDAC3: A Multifaceted Modulator in Immunotherapy Sensitization
Han, R., Luo, Y., Gao, J., Zhou, H., Wang, Y., Chen, J., Zheng, G., & Ling, C. (2025) · Vaccines · doi:10.3390/vaccines13020182 · Cited by 7 · see citing works
The NCOR-HDAC3 co-repressive complex modulates the leukemogenic potential of the transcription factor ERG
Kugler, E., Madiwale, S., Yong, D., Thoms, J. A. I., Birger, Y., Sykes, D. B., Schmoellerl, J., Drakul, A., Priebe, V., Yassin, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41067-2 · Cited by 7 · see citing works
Expression and Regulation Network of HDAC3 in Acute Myeloid Leukemia and the Implication for Targeted Therapy Based on Multidataset Data Mining
Li, M., Lan, F., Li, C., Li, N., Chen, X., Zhong, Y., Yang, Y., Shao, Y., Kong, Y., Li, X., et al. (2022) · Computational and Mathematical Methods in Medicine · doi:10.1155/2022/4703524 · Cited by 7 · see citing works
Retracted
Disruption of mitochondrial oxidative phosphorylation by chidamide eradicates leukemic cells in AML
Wang, J., Xu, J., Long, Z., & Weng, J. (2023) · Clinical & Translational Oncology · doi:10.1007/s12094-023-03079-8 · Cited by 6 · see citing works
Probing the mechanisms of hydrazide-based HDAC inhibitors binding to HDAC3 using Gaussian accelerated molecular dynamics (GaMD) simulations
Guo, F., Yang, H., Bai, X., Li, J., Han, W., & Li, W. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2278085 · Cited by 6 · see citing works
Co‐targeting driver pathways in prostate cancer: two birds with one stone
Zoubeidi, A., & Gleave, M. E. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201808928 · Cited by 6 · see citing works
Investigating the binding mechanism of AML inhibitors based on panobinostat with HDAC3 proteins using Gaussian accelerated molecular dynamics
Yu, X., Yang, H., Xue, B., Liu, T., Zhang, X., Xu, Y., Zhao, X., & Yue, X. (2025) · RSC Advances · doi:10.1039/d5ra01129a · Cited by 5 · see citing works
CD37 regulates the self-renewal of leukemic stem cells via integrin-mediated signaling in acute myeloid leukemia
Lu, J., Lv, L., Tian, X., Li, Z., Ma, Y., Li, N., Wang, J., Wang, G., Zeng, Y., Zhang, W., et al. (2025) · Stem Cell Reports · doi:10.1016/j.stemcr.2025.102476 · Cited by 4 · see citing works
Targeting HDAC8 sensitizes tyrosine kinase inhibitors in the elimination of B-cell acute lymphoblastic leukemia cells through degradation of HIF-1α
Xu, G., Wang, F., Chen, M., Gao, W., Liu, Y., Zhu, J., Wang, C., Jiang, H., Li, Y., Zhang, P., et al. (2025) · Leukemia · doi:10.1038/s41375-025-02749-6 · Cited by 4 · see citing works
Therapies of Hematological Malignancies: An Overview of the Potential Targets and Their Inhibitors
Banerjee, S., Amin, S. A., & Jha, T. (2021) · Current Chemical Biology · doi:10.2174/2212796815666210203104446 · Cited by 4 · see citing works
Chidamide enhances the sensitivity of gastric cancer to 5-fluorouracil chemotherapy by suppressing the HDAC3/HNF4A/TYMS axis
Zhang, X., Shi, L., Gao, Y., Zhou, C., Wang, X., & Shi, X. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08247-y · Cited by 2 · see citing works
Design, synthesis, and biological evaluation of novel HDAC3 PROTACs for combined therapy with Venetoclax in acute myeloid leukemia
Chen, Y., Liu, E., Ding, X., Qin, C., Jiang, Y., & Li, X. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.109520 · Cited by 2 · see citing works
Epigenetics in Acute Myeloid Leukemia
Giorgio, C., Dell’Aversana, C., & Altucci, L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803239-8.00027-2 · Cited by 2 · see citing works
PDCD5 says no to NO
Riascos‐Bernal, D. F., Sibinga, N. E. S., & Kitsis, R. N. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1804491115 · Cited by 2 · see citing works
LINC01021 Attenuates Expression and Affects Alternative Splicing of a Subset of p53-Regulated Genes
Kaller, M., Forné, I., Imhof, A., & Hermeking, H. (2024) · Cancers · doi:10.3390/cancers16091639 · Cited by 1 · see citing works
Zinc Finger Protein 82 regulates p53 protein stability through histone deacetylase and enhances neo-adjuvant chemotherapy in esophageal cancer
Peng, W., Wang, H., Sun, X., Xu, Z., Zhang, L., & Ye, L. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07979-1 · Cited by 1 · see citing works
Polyphenolic compounds remodeling acetylation modifications: Unveiling potential therapeutic strategies for hematologic malignancies
Du, Y., LIU, Q., Yao, X., Zhang, M., Yao, Y., & Sun, C. (2026) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2026.101627 · Cited by 1 · see citing works
Ara-C elicits apoptosis and inhibits proliferation of human lymphoblastic leukemia Nalm6 cell lines by down regulation of HDAC3 and DNMT3B and up regulation of DNMT3A
Moghadasi, S., Pourrajab, F., & Hekmatimoghaddam, S. (2021) · Annals of Cancer Research and Therapy · doi:10.4993/acrt.29.47 · Cited by 1 · see citing works
Reinforced erythroid differentiation inhibits leukemogenic potential of t(8;21) leukemia
Wang, M., Li, Y., Chen, J., Zhao, J., Zhu, J., & Yu, S. (2022) · The FASEB Journal · doi:10.1096/fj.202200026rr · Cited by 1 · see citing works
[Chidamide inhibits proliferation and promotes apoptosis of esophageal squamous cell carcinoma cells by inhibiting the PI3K/Akt and ERK1/2 pathways and increasing DNA damage].
Gao, M., Zhao, B., Yang, W., Tang, J., & Liu, Y. (2023) · PubMed Central · doi:10.12122/j.issn.1673-4254.2023.11.13 · Cited by 1 · see citing works
Radon Exposure and Risk of Leukemia: A Protocol of Systematic Review and Meta-Analysis
Soleimani, Y., Daraei, M., Sadeghi, P., Hajizadehanari, N., Darvishinia, A., Yasini, R., Sabeti, S., Nazari, A., & Jarrahi, A. M. (2024) · Asian Pacific Journal of Environment and Cancer · doi:10.31557/apjec.2024.7.1.99-102 · Cited by 1 · see citing works
[Advances in the mouse models of myeloid leukemia].
Ge, C.-T., & Fu, C. (2019) · PubMed Central · doi:10.7507/1001-5515.201903012 · Cited by 1 · see citing works
Analysis of the Bach2 and HDAC3 Expression in Iranian Patients with Acute Myeloid Leukemia
Safari, I., Nourian, M., Naghoosi, H., Etemadi, A., Zeinali, F., Jalaeikhoo, H., & Rajaeinejad, M. (2019) · International Journal of Cancer Management · doi:10.5812/ijcm.91545
Epigenetics in acute myeloid leukemia
Dell’Aversana, C., Giorgio, C., Tambaro, F. P., Sgueglia, G., & Altucci, L. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-823928-5.00004-9
Spatiotemporal 7q11.23 Protein Network Implicates the GTF2I-PRKDC-DDR Pathway During Early-Fetal Brain Development in Psychiatric DiseasesPreprint
Lin, G. N., Chen, L., Wang, W., Cai, W., Song, W., & Qian, W. (2020) · Research Square · doi:10.21203/rs.3.rs-93461/v1
Nrf2 overexpression increases risk of high tumor mutation burden in acute myeloid leukemia through inhibiting MSH2Preprint
Liu, P., Ma, D., Wang, P., Pan, C., Fang, Q., & Wang, J. (2020) · Research Square · doi:10.21203/rs.3.rs-66229/v1
Epigenetics
Isachesku, E., Braicu, C., Pop, L., Berindan‐Neagoe, I., & Stefan, D. C. (2022) · Cognitive systems monographs · doi:10.1007/978-3-031-17678-4_10
Clinical Studies and Epi-Drugs in Various Cancer Types
Bahsi, T., Çevik, E., Özdemir, Z. T., & Erdem, H. B. (2023) · Epigenetics and human health · doi:10.1007/978-3-031-42365-9_5
Additional file 5 of Post-translational modification of CDK1–STAT3 signaling by fisetin suppresses pancreatic cancer stem cell properties
Xu, X., Ding, Y., Jin, J., Xu, C., Hu, W., Wu, S., Ding, G., Cheng, R., Cao, L., & Jia, S. (2023) · Figshare · doi:10.6084/m9.figshare.24189127
Additional file 2 of Post-translational modification of CDK1–STAT3 signaling by fisetin suppresses pancreatic cancer stem cell properties
Xu, X., Ding, Y., Jin, J., Xu, C., Hu, W., Wu, S., Ding, G., Cheng, R., Cao, L., & Jia, S. (2023) · Figshare · doi:10.6084/m9.figshare.24189118
Additional file 4 of Post-translational modification of CDK1–STAT3 signaling by fisetin suppresses pancreatic cancer stem cell properties
Xu, X., Ding, Y., Jin, J., Xu, C., Hu, W., Wu, S., Ding, G., Cheng, R., Cao, L., & Jia, S. (2023) · Figshare · doi:10.6084/m9.figshare.24189124
Additional file 3 of Post-translational modification of CDK1–STAT3 signaling by fisetin suppresses pancreatic cancer stem cell properties
Xu, X., Ding, Y., Jin, J., Xu, C., Hu, W., Wu, S., Ding, G., Cheng, R., Cao, L., & Jia, S. (2023) · Figshare · doi:10.6084/m9.figshare.24189121
Additional file 1 of Post-translational modification of CDK1–STAT3 signaling by fisetin suppresses pancreatic cancer stem cell properties
Xu, X., Ding, Y., Jin, J., Xu, C., Hu, W., Wu, S., Ding, G., Cheng, R., Cao, L., & Jia, S. (2023) · Figshare · doi:10.6084/m9.figshare.24189112
Dual SYK-HDAC Inhibitor Elicits Striking Efficacy against Acute Myeloid Leukemia: Rational Design, Synthesis, and Biological Evaluation
Mishra, A., Yang, W.-B., Liu, T.-S., Thakur, A., Grewal, A. S., Marczyk, J., Stelitano, G., Sharma, R., Rana, M., Singh, G., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6c00039
An AI-Assisted Workflow for Rapid Prioritization of FDA-Approved Drugs as HDAC3 Inhibitor Candidates for Drug Repurposing
Kunimoto, A., Kouznetsova, V. L., Kesari, S., & Tsigelny, I. F. (2026) · Biology · doi:10.3390/biology15181570
Protein post-translational modification networks in cancer drug resistance: From mechanisms to precision targeting
Zhang, X., Yu, Y., Huang, Z., Fu, D., Wang, J., Zeng, A., & Song, L. (2026) · Genes & Diseases · doi:10.1016/j.gendis.2026.102486
HDAC inhibitors in cancer therapy: sensitization mechanisms, combination strategies, and translational challenges
Liu, K.-Y., Zhao, X., Liu, J., Li, M.-N., Cui, H., Wang, Z., & Zhou, X. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1951750
BindingDB Entry 50023081: Discovery of Highly Potent and Orally Bioavailable Histone Deacetylase 3 Inhibitors as Immunomodulators and Enhancers of DNA-Damage Response in Cancer Therapy.
BindingDB (2026) · UC San Diego · doi:10.7270/q24f1wk3
BindingDB Entry 50015231: Potent Hydrazide-Based HDAC Inhibitors with a Superior Pharmacokinetic Profile for Efficient Treatment of Acute Myeloid Leukemia In Vivo.
BindingDB (2023) · UC San Diego · doi:10.7270/q28w3j6h

Targeting of PI3K/AKT signaling and DNA damage response in acute myeloid leukemia: a novel therapeutic strategy to boost chemotherapy response and overcome resistance
Estruch, M., Vittori, C., Montesinos, T. M., Reckzeh, K., & Theilgaard‐Mönch, K. (2021) · Cancer Drug Resistance · doi:10.20517/cdr.2021.76 · Cited by 17 · see citing works
Histone deacetylase inhibitor targets CD123/CD47-positive cells and reverse chemoresistance phenotype in acute myeloid leukemia
Yan, B., Chen, Q., Shimada, K., Tang, M., Li, H., Gurumurthy, A., Khoury, J. D., Xu, B., Huang, S., & Qiu, Y. (2018) · Leukemia · doi:10.1038/s41375-018-0279-6 · Cited by 57 · see citing works
Targeting leukemia stem cells with HDAC inhibitors and modulators of the DNA damage response
Grant, S. (2014) · Leukemia Supplements · doi:10.1038/leusup.2014.8 · Cited by 2 · see citing works
HDAC3 Activity is Essential for Human Leukemic Cell Growth and the Expression of β-catenin, MYC, and WT1
Beyer, M., Romanski, A., Mustafa, A. M., Pons, M., Büchler, I., Vogel, A., Pautz, A., Sellmer, A., Schneider, G., Bug, G., et al. (2019) · Cancers · doi:10.3390/cancers11101436 · Cited by 33 · see citing works
Cooperative effect of chidamide and chemotherapeutic drugs induce apoptosis by DNA damage accumulation and repair defects in acute myeloid leukemia stem and progenitor cells
Li, Y., Wang, Y., Zhou, Y., Li, J., Chen, K., Zhang, L., Deng, M., Deng, S., Li, P., & Xu, B. (2017) · Clinical Epigenetics · doi:10.1186/s13148-017-0377-8 · Cited by 73 · see citing works

Authors: Long, J., Fang, W. Y., Chang, L., Gao, W. H., Shen, Y., Jia, M. Y., Zhang, Y. X., Wang, Y., Dou, H. B., Zhang, W. J., Zhu, J., Liang, A. B., Li, J. M., & Hu, J.
Affiliations: Shanghai Jiao Tong University (CN)
Tongji University (CN)
Corresponding author: Liang, A B
Hu, Jiong
ORCID: Long, J
Shen, Y
Zhang, Y X
Wang, Y
Zhang, W J
Zhu, J
Liang, A B
Hu, Jiong
Venue: Leukemia
Publisher: Springer Science and Business Media LLC
Published: 2017-05-02
Volume: 31
Issue: 12
Pages: 2761-2770
ISSN: 0887-6924 (ISSN-L)
1476-5551
DOI: 10.1038/leu.2017.130
OpenAlex: W2610315165
Cited by: 78
References: 49
Citations by year: 2026: 7 · 2025: 8 · 2024: 3 · 2023: 11 · 2022: 6 · 2021: 14 · 2020: 8 · 2019: 9 · 2018: 9 · 2017: 1 · 2016: 1
FWCI: 3.02
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Leukemia (publishedVersion)
PubMed (publishedVersion)
Funders: National Natural Science Foundation of China
Ministry of Science and Technology of the People's Republic of China
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Health Sciences › Medicine › Hematology › Acute Myeloid Leukemia Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
Keywords: HDAC3, Akt, acute myeloid leukemia, chemoresistance, DNA damage response, histone deacetylase, Akt phosphorylation, protein-protein interaction, MLL-AF9 leukemia, apoptosis, HDAC3 inhibitors, combination therapy, genome stability
MeSH terms: Histone Deacetylase 3, Animals, Antineoplastic Agents, Disease Models, Animal, DNA Damage, DNA Repair, Drug Synergism, Female, Histone Deacetylases, Humans, Protein Binding, Leukemia, Myeloid, Acute, Drug Resistance, Neoplasm, Xenograft Model Antitumor Assays, Cell Line, Tumor, Proto-Oncogene Proteins c-akt, Mice, Protein Interaction Domains and Motifs, Gene Knockdown Techniques, Histone Deacetylase Inhibitors

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Targeting HDAC3, a new partner protein of AKT in the reversal of chemoresistance in acute myeloid leukemia via DNA damage response

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