Cited by 559Histone Deacetylase Inhibitors ResearchMicrotubule and mitosis dynamicsGenomics and Chromatin Dynamics

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Mice Lacking Histone Deacetylase 6 Have Hyperacetylated Tubulin but Are Viable and Develop Normally

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Zhang, Yu, Kwon, SoHee, Yamaguchi, Teppei, Cubizolles, Fabien, Rousseaux, Sophie, Kneissel, Michaela, Cao, Chun, Li, Na, Cheng, Hwei-Ling, Chua, Katrin, Lombard, David, Mizeracki, Adam, Matthias, Gabriele, Alt, Frederick W., Khochbin, Saadi, Matthias, Patrick·2008·Molecular and Cellular Biology

DOI 10.1128/mcb.01154-06PMC PMC2258784

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Abstract

Posttranslational modifications play important roles in regulating protein structure and function. Histone deacetylase 6 (HDAC6) is a mostly cytoplasmic class II HDAC, which has a unique structure with two catalytic domains and a domain binding ubiquitin with high affinity. This enzyme was recently identified as a multisubstrate protein deacetylase that can act on acetylated histone tails, alpha-tubulin and Hsp90. To investigate the in vivo functions of HDAC6 and the relevance of tubulin acetylation/deacetylation, we targeted the HDAC6 gene by homologous recombination in embryonic stem cells and generated knockout mice. HDAC6-deficient mice are viable and fertile and show hyperacetylated tubulin in most tissues. The highest level of expression of HDAC6 is seen in the testis, yet development and function of this organ are normal in the absence of HDAC6. Likewise, lymphoid development is normal, but the immune response is moderately affected. Furthermore, the lack of HDAC6 results in a small increase in cancellous bone mineral density, indicating that this deacetylase plays a minor role in bone biology. HDAC6-deficient mouse embryonic fibroblasts show apparently normal microtubule organization and stability and also show increased Hsp90 acetylation correlating with impaired Hsp90 function. Collectively, these data demonstrate that mice survive well without HDAC6 and that tubulin hyperacetylation is not detrimental to normal mammalian development.

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HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403
HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153
Inhibition of Histone Deacetylase 6 Acetylates and Disrupts the Chaperone Function of Heat Shock Protein 90
Bali, P., Pranpat, M., Bradner, J., Balasis, M., Fiskus, W., Guo, F., Rocha, K., Kumaraswamy, S., Boyapalle, S., Atadja, P., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500186200 · Cited by 755
HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
Zhang, Y., Li, N., Caron, C., Matthias, G., Hess, D., Khochbin, S., & Matthias, P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg115 · Cited by 740 · cited 3×
“Also, disruption of the HDAC6 gene in mouse embryonic stem cells, which led to highly increased tubulin acetylation levels, did not significantly affect cell proliferation or differentiation of these cells (42).”
Background
In vivo destabilization of dynamic microtubules by HDAC6‐mediated deacetylation
Matsuyama, A., Shimazu, T., Sumida, Y., Saito, A., Yoshimatsu, Y., Seigneurin‐Berny, D., Osada, H., Komatsu, Y., Nishino, N., Khochbin, S., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf682 · Cited by 720
Self-citation
HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination
Boyault, C., Sadoul, K., Pabion, M., & Khochbin, S. (2007) · Oncogene · doi:10.1038/sj.onc.1210614 · Cited by 397
Self-citation
Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways
Seigneurin-Berny, D., Verdel, A., Curtet, S., Lemercier, C., Garin, J., Rousseaux, S., & Khochbin, S. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.23.8035-8044.2001 · Cited by 335
Self-citation

Flagged first, then by citations

Show all 0 references

Research works printed but not linked: 35

10.1038/sj.emboj.7601210 · DOI
10.1101/gad.436407 · DOI
10.1091/mbc.e06-01-0008 · DOI · Paper page
10.1242/jcs.02425 · DOI
10.1083/jcb.129.5.1301 · DOI
10.1128/MCB.22.17.6222-6233.2002 · DOI
10.1073/pnas.96.9.4868 · DOI · Paper page
10.1073/pnas.0430973100 · DOI · Paper page
10.1078/0171-9335-00123 · DOI
10.1073/pnas.0503221102 · DOI
10.1073/pnas.172511699 · DOI
10.1126/science.1063127 · DOI · Paper page
10.1016/S0092-8674(03)00939-5 · DOI
Kozminski K. G., 1993, Cell Motil. Cytoskelet., 25, 158, 10.1002/cm.970250205 · DOI
10.1101/gad.461107 · DOI
Matthias P., Cell Cycle
10.1016/S1097-2765(03)00038-8 · DOI
10.1038/421230a · DOI · Paper page
10.1126/science.1091325 · DOI
Rolink A., 1994, Int. Immunol., 6, 1257, 10.1093/intimm/6.8.1257 · DOI
10.1038/nature04209 · DOI
10.1038/83190 · DOI
10.1016/S1074-7613(04)00078-0 · DOI
10.1242/jcs.03431 · DOI · Paper page
Valenzuela-Fernandez A., 2005, Mol. Biol. Cell, 16, 5445, 10.1091/mbc.e05-04-0354 · DOI
10.1101/gad.1412706 · DOI
10.1016/S0960-9822(00)00542-X · DOI
10.1074/jbc.274.4.2440 · DOI
10.1016/S0168-9525(03)00073-8 · DOI · Paper page
Wang S., 2004, Novartis Found. Symp., 259, 238, 10.1002/0470862637.ch18 · DOI
10.1128/MCB.22.22.7982-7992.2002 · DOI
10.1038/nrm1260 · DOI
10.1128/MCB.25.8.2873-2884.2005 · DOI
10.1016/j.molcel.2007.05.033 · DOI
10.1074/jbc.C500241200 · DOI

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“For instance, HDAC6 knockout in mice does not lead to embryonic lethality whilst HDAC6-deficient mice are viable and show hyperacetylated tubulin in most tissues (13-20).”
Background
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“Deletion of HDAC-6 causes hyperacetylation of tubulin, which is critical for cytoskeleton dynamics and the functioning of cytoplasmic proteins including the heat shock proteins.(24,25) ACY-1083 treatment indeed markedly increases tubulin acetylation.”
Background
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Lee, M. N., Koh, A., Park, D., Jang, J., Kwak, D., Jeon, H., Kim, J. J., Choi, E.-J., Jeong, H., Suh, P., et al. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.11.006 · Cited by 8
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“Another distinctive characteristic of HDAC6 is that its deletion in mice permits normal development without major organ dysfunction [31, 32].”
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“In fact, HDAC6 knock out mice possessing hyperacetylated tubulin in most tissues proved to be viable and develop normally [26].”
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“Acknowledgments: We are grateful to Patrick Matthias (Friedrich Miescher Institute for Biomedical Research) for providing the MEF lines as well as HDAC6´{´ breeding pairs.”
MethodInfluential
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Background
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“However, HDAC6-de ﬁ cient mice remain viable and develop normally, supporting its potential as a safe therapeutic target [20].”
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“HDAC6 knockout mice are viable without major physiological dysfunction, whereas HDAC1, HDAC2-, and HDAC3-knockout mice all die prenatally or immediately after birth [9,33].”
Background
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“Germline deletion of HDAC6 28 or HDAC10 31 is readily tolerated and associated with normal development.”
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“The neuroprotective effects of HDAC inhibitors are currently under preclinical investigation as disease-modifying therapy for PD [99]; however, some of their effects may be mediated by mechanisms unrelated to histone acetylation, such as microtubule stabilization [100].”
Background
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Garcha, H. K., Nawar, N., Sorger, H., Erdogan, F., Aung, M. M. K., Sedighi, A., Manaswiyoungkul, P., Seo, H., Schönefeldt, S., Pölöske, D., et al. (2022) · Pharmaceuticals · doi:10.3390/ph15111321 · Cited by 5
“Mice lacking HDAC6 have a benign phenotype with no detrimental impact on viability, fertility, or lymphoid develop ent, suggesting that selective HDAC6 inhibition is a safe therapeutic strategy [48].”
Background
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Calciolari, B., Scarpinello, G., Tubi, L. Q., Piazza, F., & Carrer, A. (2022) · Open Biology · doi:10.1098/rsob.220038 · Cited by 6
“By contrast, HDAC6 deletion in B cells has no obvious consequence [23].”
Background
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Background
FAT10 localises in dendritic cell aggresome-like induced structures and contributes to their disassembly
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“Hind legs of HDAC6deficient mice (Zhang et al., 2008) and corresponding sex- and age-matched wild-type C57BL/6 mice were kindly provided by Patrick Matthias (Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland).”
Method
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“Additionally, constitutive knockout of HDAC6 produces viable offspring with few phenotypic changes other than resilience to stress [80].”
Background
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Depetter, Y., Geurs, S., Franceus, J., Knez, D., Desmet, T., Bosscher, K. D., Wever, O. D., Gobec, S., & D’hooghe, M. (2019) · ChemistrySelect · doi:10.1002/slct.201902042 · Cited by 4
p21Cip1 regulates cell–substrate adhesion and interphase microtubule dynamics in untransformed human mammary epithelial cells
Bouchet, B. P., Fauvet, F., Grelier, G., Galmarini, C. M., & Puisieux, A. (2011) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2011.03.002 · Cited by 5
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“…with a lower risk of lethality compared to inhibition of class I HDACs; (ii) HDAC6 regulates deacetylation of multiple non-histone substrates involved in tumor initiation, migration, and metastasis; and (iii) HDAC6 participates in immunomodulatory within the tumor microenvironment [33,59,63].”
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Qu, M., Wei, D., Ke, Q., Cheng, P., Ma, Y., Afera, B., Guo, K., Li, M., Yin, X., Wang, X., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110841 · Cited by 4
“Notably, HDAC6-knockout mice develop normally (58), supporting its safety as a therapeutic target.”
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Geurs, S., Staessens, E., Bredael, K., Borghgraef, S., Ridder, J. D., Persoons, L., Jonghe, S. D., Schols, D., Mann, M. K., Harding, R., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.117208 · Cited by 4
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Fede, E. D., Lettieri, A., Taci, E., Castiglioni, S., Rebellato, S., Parodi, C., Colombo, E. A., Grazioli, P., Natacci, F., Marchisio, P., et al. (2024) · Human Genetics · doi:10.1007/s00439-024-02675-0 · Cited by 3
“Among class IIb and IV HDACs, little is known so far about HDAC10 and HDAC11, while HDAC6 is the main tubulin deacetylase implicated in cyto - skeleton regulation (Zhang et al. 2008 ).”
Background
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Chann, A. S., Charnley, M., Newton, L. M., Newbold, A., Wiede, F., Tiganis, T., Humbert, P. O., Johnstone, R. W., & Russell, S. M. (2022) · Life Science Alliance · doi:10.26508/lsa.202201645 · Cited by 4
“Mice lacking HDAC6 showed no overt T cell phenotypes (Zhang et al, 2008; Shapiro & Shapiro, 2020), and to our knowledge, the effect of acute deletion of HDAC6 or pharmacological inhibition of HDAC6 on T cell development has not 1Optical Sciences Centre, School of Science, Swinburne University of…”
Background
Protein Acetylation and the Physiological Role of HDACs
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“This analysis revealed that some HDACs, such as HDAC1 or 3, are essential genes [6, 7], while others are dispensable for development, but show specific phenotypes when ablated, for example, organism-wide increased tubulin acetylation in the case of HDAC6 knockout mice [8].”
Self-citation
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Okudaira, S., Shimizu, M., Otsuki, B., Nakanishi, R., Ohta, A., Higuchi, K., Hosokawa, M., Tsuboyama, T., & Nakamura, T. (2010) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-010-0168-1 · Cited by 4
“There are other potential candidate genes related to bone within the interval identified in this study [63–71].”
Background
Histone Deacetylases, the Erasers of the Code
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Discovery and Development of Small Molecules Targeting Epigenetic Enzymes with Computational Methods
Meng, F., Wang, C., Wan, W., Lu, W., Lu, W., & Luo, C. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802808-7.00004-6 · Cited by 5
Discovery of novel HDAC6 inhibitors based on the diphenyl-1,2,4-oxadiazole scaffold with potential efficacy in alleviating inflammation- and chemotherapy- associated mechanical hypersensitivity.
Yin, L., Yin, M., Fan, Z., Shi, Y.-X., Shan, J., Wang, L., Chen, Y., Hao, C., Zhuang, T., Liu, T., et al. (2026) · Bioorganic chemistry (Print) · doi:10.1016/j.bioorg.2026.109785 · Cited by 2
Modeling spastic paraplegia 4 with corticospinal motor neuron-enriched cortical organoids reveals genotype-phenotype and HDAC6-targetable pathology
Mohan, N., Ramakrishnan, S., Sun, X., Sun, Y., Connors, T., Chai, V. Z., Piermarini, E., Baas, P. W., Cai, J. J., Liu, M., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117036 · Cited by 3
Protective effect of new histone deacetylase 6 inhibitors in a cisplatin-induced peripheral neurotoxicity murine model
Cavaletti, G., Canta, A., Chiorazzi, A., Ballarini, E., Rodriguez, V., Scuteri, A., Nicolini, G., Malacrida, A., Cordella, P., Stevenazzi, A., et al. (2026) · PAIN Reports · doi:10.1097/pr9.0000000000001395 · Cited by 2
“…of Milano-Bicocca, Monza, Italy, b Fondazione IRCCS San Gerardo dei Tintori di Monza, Monza, Italy, c Preclinical R&D Department, Italfarmaco S.p.A., Cinisello Balsamo, Italy are viable and apparently show no gross impairments, 23 suggesting that HDAC6 inhibition should be well-tolerated.”
Unlocking the therapeutic potential of HDAC inhibitors in colorectal cancer: Mechanisms, efficacy, and future perspectives
Wen, Y., Yang, C., Ye, Y., Shen, Z., & Wang, C. (2025) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2025.104920 · Cited by 3
Design, synthesis and neuroprotective biological evaluation of novel HDAC6 inhibitors incorporating benzothiadiazinyl systems as cap groups
Han, B. R., Gu, X. Q., Wang, M., Wang, H., Sun, N., Yang, X., & Zhang, Q. (2024) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14556 · Cited by 2
“In contrast to the lethal effect of HDAC1-3 gene knockout, HDAC6 knockout mice survived normally (Zhang et al., 2008).”
Background
Upregulation of Profilin 2 on HDAC6 overexpression in mouse GC-1 cells and its putative role in germ cell migration in the testis
Verma, P., Yevate, S., Jeeva, S., & Parte, P. P. (2023) · Cell and Tissue Research · doi:10.1007/s00441-023-03755-9 · Cited by 3
“However, HDAC6-deficient mice are viable and fertile (Zhang et al. 2008).”
Background
Correction to: HDAC6 deacetylates alpha tubulin in sperm and modulates sperm motility in Holtzman rat
Parab, S., Shetty, O., Gaonkar, R., Balasinor, N., Khole, V., & Parte, P. (2017) · Cell and Tissue Research · doi:10.1007/s00441-017-2741-6 · Cited by 2
“SIRT2 is dependent on HDAC6 for tubulin deacetylation, whereas interaction between HDAC6 and tubulin has been established as being independent of other proteins (Zhang et al. 2008; Zhao et al. 2010).”
Background
Broader implications: biological and clinical significance of microtubule acetylation
Kelley, T. J., & Rymut, S. M. (2015) · Cell Health and Cytoskeleton · doi:10.2147/chc.s77040 · Cited by 4
“At a cellular level, they exhibit microtubule hyperacetylation; however, they do not show any growth defects and develop normally.(29) The lack of deleterious phenotypes and the effective modulation of microtubule regulation in the HDAC6-null mice support HDAC6 as a potential therapeutic intervention for various disea…”
Methylation and acetylation of histones during spermatogenesis
Ge, S., Li, J., & Zhang, X. (2011) · Hereditas (Beijing) · doi:10.3724/sp.j.1005.2011.00939 · Cited by 1
HDAC6 Regulation of Androgen Signaling in Prostate Cancer
Ai, J., & Wang, Z. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6828-8_16 · Cited by 1
Identification of Histone Deacetylase Inhibitor Targeting Type I Interferon and B Cell Abnormalities in Systemic Lupus Erythematosus
Hirayama, T., Konaka, H., Kato, Y., Shibahara, T., Nishizawa, C., Tsujimoto, K., Park, J., Itotagawa, E., Jo, T., Nishide, M., et al. (2025) · Arthritis & Rheumatology · doi:10.1002/art.43434 · Cited by 1
“49,50 We showed that vorinostat-treated mice were healthy, with no effect on T cell populations, anorexia, weight loss, and little off-target expression or repression of mRNAs, suggesting to be tolerable for SLE.”
Design, synthesis, and biological evaluation of quinazolin-4-one-based selective HDAC6 inhibitors targeting serine 531, histidine 614 residues, and the L1 and L2 loop
Gupta, S., Oh, Y. J., Kim, M. K., Ha, E., & Seo, Y. H. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.118184 · Cited by 1
Dispensability of Tubulin Acetylation for 15-protofilament Microtubule Formation in the Mammalian Cochlea
Renauld, J., Thelen, N., Bartholome, O., Malgrange, B., & Thiry, M. (2021) · Cell Structure and Function · doi:10.1247/csf.20057 · Cited by 1
“This data seems to show a high tolerance in the level of acetylation of microtubules in mice (Zhang et al. , 2008).”
Background
HDAC6 regulates expression of the oncogenic driver EWSR1-FLI1 through the EWSR1 promoter in Ewing sarcoma
García-Domínguez, D., Hajji, N., Sánchez-Molina, S., Figuerola-Bou, E., de Pablos, R. D., Espinosa-Oliva, A. M., Andrés-León, E., Terrón-Camero, L., Flores-Campos, R., Pascual-Pasto, G., et al. (2021) · bioRxiv · doi:10.1101/2021.01.04.425179 · Cited by 1
HDAC6-HSP90 pathway-mediated protein folding and degradation regulates tumor cell proliferation and metastasis
Tian, R., Yan, X., Yu, S., Xu, L., Zhao, Y., Sun, L., & Su, J. (2020) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/tb-2020-0644 · Cited by 1
Role of histone deacetylases 6 (HDAC6) in cancers.
Safa, A. (2017) · doi:10.35841/pharmacology.1.1.3-7 · Cited by 1
“Several studies [1,4-6] have implicated HDAC6 expression and function in regulating microtubules, growth factor-induced chemotaxis, misfolded protein stress response and tumor invasion, and it has been linked to cell transformation (Figure 1).”
Background
Epigenetic Approaches
Sahakian, E., Woan, K. V., Villagra, A., & Sotomayor, E. M. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394296-8.00022-1 · Cited by 2
KDAC6 alters cell morphology and motility through positive and negative modulation of F‐actin distribution
Joseph, T. V., Pham, A. B., Bornes, K. E., Hammad, R. H., Rousseve‐Ross, C. A., Huckaba, T. M., Watt, T. J., & Toro, T. B. (2026) · FEBS Open Bio · doi:10.1002/2211-5463.70302
“…knockout mice developed with only a few reported abnormalities that did not impact growth or fertility despite having hyperacetylated tubulin, consistent with the observed minimal impact from complete loss of KDAC6 in this work and the analogous study on inactivation of the third domain [55,71].”
Targeting HDAC6 mitigates diabetic nephropathy through modulation of oxidative stress, inflammatory pathways, and apoptotic signaling
Kim, U. J., Lee, E. K., Kim, J. R., Song, Y. J., Cho, Y. E., Kwon, O. K., Park, J. H., & Kim, H. S. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.118283
Primary cilium disassembly – from mechanisms to roles in physiology and disease
Ott, C. M., Lippincott‐Schwartz, J., & Breslow, D. K. (2026) · Journal of Cell Science · doi:10.1242/jcs.264820
“However, loss of HDAC6 or the acetyltransferase ATAT1 does not grossly alter ciliation in vivo (Bertrand and Grimes, 2026; Fukada et al., 2012; Kalebic et al., 2013; Kim et al., 2013; Lysyganicz et al., 2021; Zhang et al., 2008).”
Sirtuin 2 Regulates Dorsal Hippocampal Actin Polymerization and Microtubule Acetylation-Dependent EB3 Activation to Modulate Opioid Withdrawal–Induced Aversive Memory and Associative Learning
Long, J.-D., Yao, S.-Y., Wu, W., Zan, G., Wang, Z.-W., Wei, X., Shu, X., Chen, Y., Ju, Y., Chen, J., et al. (2026) · Biological Psychiatry · doi:10.1016/j.biopsych.2026.06.001
The role of HDAC6-mediated Prx2 acetylation in neuronal apoptosis related to Alzheimer's disease
Zhang, L., Hu, J., Zhang, T., Gao, H., Wu, X., Zhang, C., Zhang, C., Chen, H., Yang, M., Cao, X., et al. (2026) · Journal of Alzheimer s Disease · doi:10.1177/13872877251414961
“39 The mice were housed under controlled temperature, humidity and light conditions (Animals were kept under a 12 h light/dark cycle) with water and rodent chow diet freely available.”
HDAC6 Inhibition Reduces Seeded Tau and α-Synuclein Pathologies in Primary Neuron Cultures and Wild-Type Mice
Crowe, A., Yao, Y., Newman, M., Hoxha, K., Baffic, T., & Brunden, K. R. (2025) · Journal of Neuroscience · doi:10.1523/jneurosci.1092-25.2025 · Cited by 2
Mutating different α-tubulin acetylation sites has distinct effects on axon terminal morphogenesis in Drosophila melanogaster
Than, H., Welch, C. J., Schauer, E., Truijillo, S., & Wildonger, J. (2025) · bioRxiv · doi:10.1101/2025.10.27.684845
“Similarly, the deacetylase HDAC6 targets α-tubulin K40, K394, and K370 but not K326 or K401 (Hubbert et al. , 2002; Zhang et al. , 2008; Liu et al. , 2015a; Saunders et al. , 2022).”
Genotype–Phenotype Distinctions in Spastic Paraplegia 4 Reveal HDAC6 as a Therapeutic TargetPreprint
Mohan, N., Ramakrishnan, S., Sun, X., Sun, Y., Connors, T. M., Chai, V. Z., Piermarini, E., Baas, P. W., Cai, J. J., Liu, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.15.664947
Targeting histone deacetylase 6 (HDAC6) in Duchenne muscular dystrophy: New insights into therapeutic potential
Osseni, A., & Schaeffer, L. (2024) · Acta Physiologica · doi:10.1111/apha.14256
Expression and cilia associated localization of Histone deacetylases 6 in Xenopus
Tisler, M., Ott, T., Blum, M., & Schweickert, A. (2023) · microPublication Biology · doi:10.17912/micropub.biology.000919
“Although lacking an obvious developmental phenotype, HDAC6 depleted mice show defects in bone mineralization and alterations regarding the immune response and emotional behavior (Fukada et al., 2012; Zhang et al., 2008).”
BackgroundResult
Identification of HDAC10 Inhibitors that Modulate Autophagy-Related Proteins in Transformed CellsPreprint
Zeyen, P., Zeyn, Y., Herp, D., Mahmoudi, F., Yesiloglu, T. Z., Erdmann, F., Schmidt, M., Robaa, D., Romier, C., Ridinger, J., et al. (2022) · ChemRxiv · doi:10.26434/chemrxiv-2022-kh906
Post-Translational Tubulin Modifications in Differentiated Human Neural Stem CellsPreprint
Knight, V. B., Jogalekar, M. P., & Serrano, E. E. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.31.474563
“While posttranslational tubulin modifications have been explored in the pre-implantation embryo and through the development of knockout mice, there is a paucity of information about the posttranslational modification profiles of tubulin in differentiating stem cells (Houliston & Maro, 1989; Zhang et al., 2008).”
Background
Stepwise progression of β-selection during T cell development as revealed by histone deacetylation inhibition
Chann, A. S., Charnley, M., Newton, L. M., Newbold, A., Wiede, F., Tiganis, T., Humbert, P., Johnstone, R., & Russell, S. (2021) · bioRxiv · doi:10.1101/2021.10.03.462949
“Mice lacking HDAC6 showed no overt T cell phenotypes (Shapiro and Shapiro, 2020; Zhang et al., 2008) and to our knowledge the effect of acute deletion of HDAC6, or pharmacological inhibition of HDAC6 on T cell development has not been reported (Shapiro and Shapiro, 2020).”
Background
The short chain fatty acid butyrate prevents intracellular replication of Legionella by regulating cysteine levels in macrophagesPreprint
Abraham, G., Swaminathan, A., Barlow, C. K., Nguyen, T. N., Bhuvan, T., Heng, T. S. P., Lazarou, M., Kapétanovic, R., Sweet, M. J., Traven, A., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-829027/v1 · Cited by 2
“Cell culture 475 Murine bone marrow-derived macrophages (BMDMs) were obtained from femur and tibia of 476 female/male 6-8-week-old C57BL/6 WT or HDAC6 mice (59).”
Method
Restoring vascular endothelial autophagic flux reduces atherosclerotic lesionsPreprint
Chatterjee, S., Kheloufi, M., Mazlan, S. M. I., Loyer, X., McKinsey, T. A., Boulanger, C. M., & Coly, P. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.06.442901
Functional role of increased acetylated tubulin in porcine oocyte microtubule structure, meiotic maturation and embryogenesisPreprint
Sun, J., Cui, K., Li, Z., Gao, B., Jiang, J., Liu, Q., Huang, B., & Shi, D. (2019) · doi:10.21203/rs.2.19001/v1
“HDAC6 knockout in mice increased microtubules acetylation without affecting the growth and development(22).”
Background
Developmental Testicular Expression, Cloning, and Characterization of Rat HDAC6 In Silico
Verma, P., Shetty, O. A., Parab, S., Menezes, K., & Parte, P. P. (2017) · BioMed Research International · doi:10.1155/2017/5170680 · Cited by 1
Rôle du cil primaire au cours de la différenciation adipocytaire
Forcioli-Conti, N. (2015) · theses.fr (ABES) · doi:10.70675/3aaca85ezf2c0z4f6dza030z6d71a2a6263d
The Cancer Super-Chaperone Hsp90: Its Posttranslational Regulation and Drug Targeting
Walton-Diaz, A., Khan, S., Trepel, J., Mollapour, M., & Neckers, L. (2013) · doi:10.1201/b15944-12
Advances in Induced Pluripotent Stem Cell Technologies
Pal, R., Rao, M. S., Vemuri, M. C., Verma, P. J., & Dinnyés, A. (2012) · Stem Cells International · doi:10.1155/2012/850201 · Cited by 1
Gestörte epigenetische Regulation als Angriffspunkt für neue Substanzen zur Behandlung von Demenzen und Psychosen
Fischer, A., & Falkai, P. (2011) · Die Psychiatrie · doi:10.1055/s-0038-1671899
“Das am Besten charakterisierte HDAC6 Substrat ist Tubulin (66).”
Background
The role of epigenetic regulation in cancer
Zhang, J., Yang, C., & Wu, C. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-823684-0.00005-0
Implications of Primary Cilia and Associated Lysophosphatidic Acid Signaling in Glioblastoma Biology and Therapy
Loskutov, Y. V. (2017) · The Research Repository @ WVU (West Virginia University) · doi:10.33915/etd.6113
Function and Regulation of the Tip60-p400 Complex in Embryonic Stem Cells: A Dissertation
Chen, P. B. (2015) · eScholarship@UMassChan · doi:10.13028/m2sw20
“, 2009), Hdac6 KO ESCs can self-renew and are competent for mouse development (Zhang et al., 2008), strongly suggesting that the defect observed for Hdac6 KD ESCs in vitro is overcome in the embryo by compensatory mechanisms.”
Background
Targeting Selective Autophagy of Insoluble Protein Aggregates
Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801944-3.00005-9
Selective Disposal of Insoluble Protein Aggregates
Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800186-8.00005-5 · Cited by 1
Epigenetic regulation of thyroid development
Gawade, S. (2015) · doi:10.5451/unibas-006625818
Epigenetics and Cardiovascular Disease
Marı́n-Garcı́a, J. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-404599-6.00022-6
HDAC6 activity is required for efficient polarization and intracellular transport of organelles in directionally migrating cells
Salam, A. (2013) · doi:10.7916/d8kd257d
“This prediction is amenable to test, using mice null for HDAC6 (Gao et al., 2007; Zhang et al., 2008) and SIRT2 (Vaquero et al.”
BackgroundMethodResultInfluential
Dissecting the roles of histone deacetylase 1 and 2 in the hematopoietic system
Yamaguchi, T. (2008) · doi:10.5451/unibas-004690321
Self-citation

Authors: Zhang, Y., Kwon, S., Yamaguchi, T., Cubizolles, F., Rousseaux, S., Kneissel, M., Cao, C., Li, N., Cheng, H.-L., Chua, K., Lombard, D., Mizeracki, A., Matthias, G., Alt, F. W., Khochbin, S., & Matthias, P.
Affiliations: Friedrich Miescher Institute (CH)
Friedrich Miescher Institute for Biomedical Research, Novartis Research Foundation, P.O. Box 2543, Maulbeerstrasse 66, 4058 Basel, Switzerland
Inserm (FR)
Novartis (Switzerland) (CH)
Howard Hughes Medical Institute (US)
Corresponding author: Matthias, Patrick
ORCID: Zhang, Yu
Yamaguchi, Teppei
Cubizolles, Fabien
Rousseaux, Sophie
Kneissel, Michaela
Li, Na
Cheng, Hwei-Ling
Chua, Katrin
Lombard, David
Matthias, Gabriele
Alt, Frederick W.
Khochbin, Saadi
Matthias, Patrick
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2008-03-01
Volume: 28
Issue: 5
Pages: 1688-1701
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.01154-06
PMC: PMC2258784
OpenAlex: W2162787110
Cited by: 559
References: 0
Citations by year: 2026: 19 · 2025: 28 · 2024: 18 · 2023: 24 · 2022: 37 · 2021: 35 · 2020: 47 · 2019: 32 · 2018: 27 · 2017: 38 · 2016: 24 · 2015: 28 · 2014: 32 · 2013: 33 · 2012: 39
FWCI: 13.59
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: Howard Hughes Medical Institute
Ellison Medical Foundation
Dalhousie University
Université de Fribourg
Institut National Du Cancer
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: HDAC6, tubulin acetylation, tubulin deacetylation, alpha-tubulin, HSP90 acetylation, testicular development, lymphoid development, immune response, bone mineral density, microtubule organization, embryonic fibroblasts, post-translational modification, ubiquitin binding
MeSH terms: Histone Deacetylase 6, Acetylation, Animals, Cells, Cultured, Crosses, Genetic, Embryo, Mammalian, Female, Fetal Viability, Fibroblasts, Histone Deacetylases, Homozygote, Immunohistochemistry, Male, Mice, Inbred C57BL, Precipitin Tests, Pregnancy, Receptors, Glucocorticoid, Recombination, Genetic, Sperm Count, Spermatogenesis, Testis, Transfection, Tubulin, Absorptiometry, Photon, Bone Density, Gene Deletion, Genes, Reporter, Mice, Knockout, HSP90 Heat-Shock Proteins, Fluorescent Antibody Technique, Indirect, NIH 3T3 Cells, Embryonic Development, Luciferases, Renilla, Mice, Embryonic Stem Cells

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Mice Lacking Histone Deacetylase 6 Have Hyperacetylated Tubulin but Are Viable and Develop Normally

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