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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Background
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Background
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BackgroundInfluential
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Background
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“(45) showed that germline HDAC6 deletion modestly”
Self-citation
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“in hdac6 knockout mice.(45) In addition, class I HDACi such as Romidepsin, which induces a thrombocytopenia, have a minor effect on HDAC6.”
Background
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Background
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“viable, fertile, and appear to have no overall phenotype, and in fact, have been reported to manifest enhanced cognition [185,186].”
Background
RETRACTED ARTICLE: Disruption of lipid-raft localized Gαs/tubulin complexes by antidepressants: a unique feature of HDAC6 inhibitors, SSRI and tricyclic compounds
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“HDAC6 KO mice show increased amounts of acetylated α -tubulin in different tissues, including brain [55].”
Retracted
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Histone deacetylase 6 inhibition counteracts the epithelial-mesenchymal transition of peritoneal mesothelial cells and prevents peritoneal fibrosis
Xu, L., Liu, N., Gu, H., Wang, H., Shi, Y., Ma, X., Ma, S., Ni, J., Tao, M., Qiu, A., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.20982 · Cited by 35
“Since HDAC6 KO mice do not show abnormal function of major organs [31], there may promise in developing HDAC6 inhibitors as drugs for use in the prevention and/or treatment of chronic complications like peritoneal fibrosis.”
Background
An inhibitor of histone deacetylase 6 activity, ACY-1215, reduces cAMP and cyst growth in polycystic kidney disease
Yanda, M. K., Liu, Q., & Cebotaru, L. (2017) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00186.2017 · Cited by 35
p27 controls autophagic vesicle trafficking in glucose-deprived cells via the regulation of ATAT1-mediated microtubule acetylation
Nowosad, A., Creff, J., Jeannot, P., Culerrier, R. M., Codogno, P., Manenti, S., Nguyen, L., & Besson, A. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03759-9 · Cited by 131
Neuronal complexity is attenuated in preclinical models of migraine and restored by HDAC6 inhibition
Bertels, Z., Singh, H., Dripps, I. J., Siegersma, K., Tipton, A. F., Witkowski, W., Sheets, Z. C., Shah, P. V., Conway, C. M., Mangutov, E., et al. (2021) · eLife · doi:10.7554/elife.63076 · Cited by 57
“Additionally, constitutive knockout of HDAC6 produces viable offspring with few phenotypic changes (Zhang et al., 2008).”
Background
HDAC6 Inhibition Alleviates CLL-Induced T-Cell Dysfunction and Enhances Immune Checkpoint Blockade Efficacy in the Eμ-TCL1 Model
Maharaj, K. K., Powers, J. J., Mediavilla-Varela, M., Achille, A. N., Gamal, W. M., Quayle, S. N., Jones, S. S., Sahakian, E., & Pinilla-Ibarz, J. A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.590072 · Cited by 34
“CLL Mouse Model An HDAC6-deficient CLL murine model (Em-TCL1/ HDAC6KO) was generated by crossing HDAC6KO (18) and Em-TCL1 (19) (C57BL/6 background) mice.”
Method
Impaired autophagy triggered by HDAC9 in mesenchymal stem cells accelerates bone mass loss
Zhang, L., Qi, M., Chen, J., Zhao, J., Li, L., Hu, J.-C. E., Jin, Y. J., & Liu, W. (2020) · Stem Cell Research & Therapy · doi:10.1186/s13287-020-01785-6 · Cited by 37
HDAC expression and activity is upregulated in diseased lupus-prone mice
Regna, N. L., Vieson, M. D., Gojmerac, A. M., Luo, X., Caudell, D. L., & Reilly, C. M. (2015) · International Immunopharmacology · doi:10.1016/j.intimp.2015.10.006 · Cited by 30
Chiral Mercaptoacetamides Display Enantioselective Inhibition of Histone Deacetylase 6 and Exhibit Neuroprotection in Cortical Neuron Models of Oxidative Stress
Kalin, J. H., Zhang, H., Gaudrel‐Grosay, S., Vistoli, G., & Kozikowski, A. P. (2012) · ChemMedChem · doi:10.1002/cmdc.201100522 · Cited by 36
Discovery of HDAC6-Selective Inhibitor NN-390 with in Vitro Efficacy in Group 3 Medulloblastoma
Nawar, N., Bukhari, S., Adile, A., Suk, Y., Manaswiyoungkul, P., Toutah, K., Olaoye, O. O., Raouf, Y. S., Sedighi, A., Garcha, H. K., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01585 · Cited by 38
HDAC6 Degradation Inhibits the Growth of High-Grade Serous Ovarian Cancer Cells
Ali, A., Zhang, F., Maguire, A., Byrne, T., Weiner‐Gorzel, K., Bridgett, S., O’Toole, S. A., O’Leary, J. J., Beggan, C., Fitzpatrick, P., et al. (2020) · Cancers · doi:10.3390/cancers12123734 · Cited by 36
Histone deacetylase 6 inhibition reduces cysts by decreasing cAMP and Ca2+ in knock-out mouse models of polycystic kidney disease
Yanda, M. K., Liu, Q., Cebotaru, V., Guggino, W. B., & Cebotaru, L. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.803775 · Cited by 40
“Interestingly, mice lacking HDAC6 are viable and fertile and have no gross morphological abnormalities (45); this observation has important implications for the safety of potential therapeutic inhibition of HDAC6.”
Background
The size of the primary cilium and acetylated tubulin are modulated during adipocyte differentiation: Analysis of HDAC6 functions in these processes
Forcioli-Conti, N., Estève, D., Bouloumié, A., Dani, C., & Peraldi, P. (2015) · Biochimie · doi:10.1016/j.biochi.2015.09.011 · Cited by 31
HDAC6 and Ovarian Cancer
Haakenson, J., & Zhang, X. M. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14059514 · Cited by 31
“It seems to play a bigger role in bone development, where decreased HDAC6 results in increased cancellous bone mineral density [79].”
Background
Inhibitors selective for HDAC6 in enzymes and cells
Gupta, P. K., Reid, R. C., Liu, L., Lucke, A. J., Broomfield, S., Andrews, M. R., Sweet, M. J., & Fairlie, D. P. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.09.100 · Cited by 31
Histone deacetylase 6 (HDAC6) is an essential factor for oocyte maturation and asymmetric division in mice
Zhou, D., Choi, Y., & Kim, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-08650-2 · Cited by 35
HDAC6 regulates NF-κB signalling to control chondrocyte IL-1-induced MMP and inflammatory gene expression
Barter, M. J., Butcher, A., Wang, H., Tsompani, D., Galler, M., Rumsby, E. L., Culley, K. L., Clark, I. M., & Young, D. A. (2022) · Scientific Reports · doi:10.1038/s41598-022-10518-z · Cited by 34
Targeting the photoreceptor cilium for the treatment of retinal diseases
Ran, J., & Zhou, J. Y. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-0486-3 · Cited by 29
“HDAC6-deficient mice also appear to be superficially normal under standard laboratory conditions [69].”
Background
Cortactin deacetylation by HDAC6 and SIRT2 regulates neuronal migration and dendrite morphogenesis during cerebral cortex development
Kim, J.-Y., Hwang, H.-G., Lee, J., Kim, J., & Kim, J. (2020) · Molecular Brain · doi:10.1186/s13041-020-00644-y · Cited by 34
Profiling of human epigenetic regulators using a semi-automated real-time qPCR platform validated by next generation sequencing
Dudakovic, A., Gluscevic, M., Paradise, C. R., Dudakovic, H., Khani, F., Thaler, R., Ahmed, F. S., Li, X., Dietz, A. B., Stein, G. S., et al. (2017) · Gene · doi:10.1016/j.gene.2017.01.019 · Cited by 29
“…knockout, knock-down or chemical inhibition in mouse models typically has negative effects on skeletal development and bone mineral density (Bradley et al., 2015; Gordon et al., 2015; McGee-Lawrence et al., 2011; Pratap et al., 2010; Razidlo et al., 2010; Senn et al., 2010; Zhang et al., 2008).”
Synthesis of benzothiophene-based hydroxamic acids as potent and selective HDAC6 inhibitors
Vreese, R. D., Steen, N. V., Verhaeghe, T., Desmet, T., Bougarne, N., Bosscher, K. D., Benoy, V., Haeck, W., Bosch, L. V. D., & D’hooghe, M. (2015) · Chemical Communications · doi:10.1039/c5cc03295d · Cited by 32
Adult-onset Alexander disease, associated with a mutation in an alternative GFAP transcript, may be phenotypically modulated by a non-neutral HDAC6 variant
Melchionda, L., Fang, M., Wang, H., Fugnanesi, V., Morbin, M., Liu, X., Li, W., Ceccherini, I., Farina, L., Savoiardo, M., et al. (2013) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-8-66 · Cited by 24
“As for mammalian models, although a first strain of HDAC6 knockout (KO) mice presented no sign of neurodegeneration, [29] altered emotional behaviors suggested a contribution of HDAC6 to maintain proper neuronal activity [30].”
Background
Depression of mitochondrial metabolism by downregulation of cytoplasmic deacetylase, HDAC6
Kamemura, K., Ogawa, M., Ohkubo, S., Ohtsuka, Y., Shitara, Y., Komiya, T., Maeda, S., Ito, A., & Yoshida, M. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.03.060 · Cited by 29
“HDAC6-deficient mouse embryonic fibroblast (MEF) cell line is described in the literature [15].”
Background
Polarity in Cell-Fate Acquisition in the Early Mouse Embryo
Leung, C. Y., Zhu, M., & Zernicka‐Goetz, M. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.04.008 · Cited by 41
Macrophage migration inhibitory factor (MIF) acetylation protects neurons from ischemic injury
Hu, J., Ma, W.-J., He, L., Zhang, C.-H., Zhang, C., Wang, Y., Chen, C.-N., Shen, D., Gao, H.-M., Guo, R.-R., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04918-2 · Cited by 30
“RESULTS HDAC6 suppression protects against ischemia-induced brain injury HDAC6 is expressed in the mouse brain [27].”
Background
Roles for α-Synuclein in Gene Expression
Somayaji, M., Lanseur, Z., Choi, S. J., Sulzer, D., & Mosharov, E. V. (2021) · Genes · doi:10.3390/genes12081166 · Cited by 32
“Although pharmacological inhibition of HDAC activity is currently under investigation as disease modifying PD therapy [100,109], some of their effects may be mediated by mechanisms unrelated to histone acetylation, such as microtubule stabilization [110,111].”
Background
Opportunities for histone deacetylase inhibition in amyotrophic lateral sclerosis
Klingl, Y. E., Pakravan, D., & Bosch, L. V. D. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15217 · Cited by 33
“Genetic ablation as well as nuclear localization of HDAC1 was neuroprotective (Zhu et al., 2017).”
Background
Amyotrophic Lateral Sclerosis Modifiers inDrosophilaReveal the Phospholipase D Pathway as a Potential Therapeutic Target
Kankel, M. W., Sen, A., Lü, L., Theodorou, M., Dimlich, D. N., McCampbell, A., Henderson, C. E., Shneider, N. A., & Artavanis‐Tsakonas, S. (2020) · Genetics · doi:10.1534/genetics.119.302985 · Cited by 35
The histone deacetylase inhibitor tubacin mitigates endothelial dysfunction by up-regulating the expression of endothelial nitric oxide synthase
Chen, J., Zhang, J., Shaik, N. F., Yi, B., Wei, X., Yang, X., Naik, U. P., Summer, R. S., Yan, G., Xu, X., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011317 · Cited by 36
“Among 18 HDACs in mammals, HDAC6 is a unique member of the type II HDACs that has been shown to regulate cytoskeleton dynamics by acting as a specific -tubulin deacetylase (18, 22), which prompted us to investigate whether inhibition of HDAC6 could alter eNOS gene expression through modulating cytoskeleton dynamics in…”
Background
Histone deacetylase 6 regulates cytokinesis and erythrocyte enucleation through deacetylation of formin protein mDia2
Li, X., Mei, Y., Yan, B., Vitriol, E. A., Huang, S., Ji, P., & Qiu, Y. (2017) · Haematologica · doi:10.3324/haematol.2016.161513 · Cited by 34
“It is worth mentioning that HDAC6 knockout mice are viable with no developmental defect.(23,43) Although the mice have hyperacetylated tubulin and elevated acetylated HSP90, they do not have significant cellular defects, as shown in transient knockdown cell lines,(18,43) suggesting that germline deletion of HDAC6 may…”
Background
Psychiatric behaviors associated with cytoskeletal defects in radial neuronal migration
Fukuda, T., & Yanagi, S. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2539-4 · Cited by 31
“HDAC6 knockout mice are reported to be viable and fertile, and show no obvious phenotypic changes [145].”
Understanding Histone Deacetylases in the Cancer Development and Treatment: An Epigenetic Perspective of Cancer Chemotherapy
Ahmad, M., Hamid, A., Hussain, A., Majeed, R., Qurishi, Y., Bhat, J. A., Najar, R. A., Qazi, A. K., Zargar, M. A., Singh, S. K., et al. (2012) · DNA and Cell Biology · doi:10.1089/dna.2011.1575 · Cited by 27
Protein lysine acetylation and its role in different human pathologies: a proteomic approach
Morales-Tarré, O., Alonso-Bastida, R., Arcos-Encarnación, B., Pérez‐Martínez, L., & Encarnación‐Guevara, S. (2021) · Expert Review of Proteomics · doi:10.1080/14789450.2021.2007766 · Cited by 30
“This HADC, primarily localized in the cytoplasm, is the only HDAC described so far that possesses a C-terminal zinc finger and two deacetylase domains [62].”
Background
The emerging role of tubulin posttranslational modifications in cilia and ciliopathies
He, K., Ling, K., & Hu, J. (2020) · Biophysics Reports · doi:10.1007/s41048-020-00111-0 · Cited by 25
The Selective HDAC6 Inhibitor ACY-738 Impacts Memory and Disease Regulation in an Animal Model of Multiple Sclerosis
LoPresti, P. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00519 · Cited by 30
Author Correction: Selective HDAC6 inhibitors improve anti-PD-1 immune checkpoint blockade therapy by decreasing the anti-inflammatory phenotype of macrophages and down-regulation of immunosuppressive proteins in tumor cells
Knox, T. J., Sahakian, E., Banik, D., Hadley, M. M., Palmer, E., Noonepalle, S. K. R., Kim, J. S., Powers, J. J., Gracia-Hernandez, M., Oliveira, V. A., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-51403-6 · Cited by 118
Developing selective histone deacetylases (HDACs) inhibitors through ebselen and analogs
Wang, Y., Wallach, J. V., Duane, S., Wang, Y., Wu, J., Wang, J., Adejare, A., & Ma, H. (2017) · Drug Design Development and Therapy · doi:10.2147/dddt.s124977 · Cited by 32
“Mice lacking HDAC6 are viable and have greatly elevated tubulin acetylation in multiple organs.(27) In addition, they exhibit a moderately impaired immune response and bone homeostasis.”
The tubulin deacetylase sirtuin-2 regulates neuronal differentiation through the ERK/CREB signaling pathway
Jeong, S., & Cho, G. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.11.031 · Cited by 29
Epigenetic regulation by DNA methylation, histone modifications and chromatin remodeling complexes in controlling spermatogenesis and their dysfunction with male infertility
Cui, Y., Deng, J., Zhang, Y., Du, L., Jiang, F., Li, C., Chen, W., Zhang, H., & He, Z. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05831-5 · Cited by 28
“…earliest identified PTMs affecting transcriptional regulation, adds negative changes Transcriptional activation Hdac6 -deficient mice are fertile [ 92]; Tip60 −/− mice appear to be arrested at the round spermatids [90]. are lost, which facilitates genome-wide DNA demethylation and epigenetic…”
Self-citation
CAMSAP1 role in orchestrating structure and dynamics of manchette microtubule minus-ends impacts male fertility during spermiogenesis
Hu, W., Zhang, R., Xu, H., Li, Y., Yang, X.-J., Zhou, Z., Huang, X., Wang, Y., Ji, W., Gao, F., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313787120 · Cited by 32
“Analogously, previous studies have reported that mice lacking HDAC6 (Histone Deacetylase 6) exhibit hyperacetylated microtubules, but it does not affect testis architecture, fertility, and sperm count (36).”
Background
Dendropanoxide Alleviates Thioacetamide-induced Hepatic Fibrosis via Inhibition of ROS Production and Inflammation in BALB/C Mice
Kundu, A. B., Gali, S., Sharma, S., Kacew, S., Yoon, S., Jeong, H. G., Kwak, J. H., & Kim, H. S. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.80743 · Cited by 31
“Upon stimulation, JNK/p38 and Smad, regulate apoptosis, whereas the activation of transcription factors leads to epithelial to mesenchymal transition (EMT) [17, 18].”
Identification of HDAC10 Inhibitors that Modulate Autophagy in Transformed Cells
Zeyen, P., Zeyn, Y., Herp, D., Mahmoudi, F., Yesiloglu, T. Z., Erdmann, F., Schmidt, M., Robaa, D., Romier, C., Ridinger, J., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114272 · Cited by 36
HDAC6 Regulates Radiosensitivity of Non-Small Cell Lung Cancer by Promoting Degradation of Chk1
Moses, N., Zhang, M., Wu, J.-Y., Chen, H., Xiang, S., Malysa, A., Jang, H., Chen, W., Bai, W., Bepler, G., et al. (2020) · Cells · doi:10.3390/cells9102237 · Cited by 28
“In particular, HDAC6 knockout mice develop normally, which makes HDAC6 an ideal target in cancer treatment [15].”
Background
MPT0G413, A Novel HDAC6-Selective Inhibitor, and Bortezomib Synergistically Exert Anti-tumor Activity in Multiple Myeloma Cells
Huang, F.-I., Wu, Y.-W., Sung, T.-Y., Liou, J., Lin, M., Pan, S., & Yang, C. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00249 · Cited by 26
“A previous report has demonstrated that HDAC6deficient mice are viable and normally develop, indicating that HDAC6 inhibition would not cause severe side effects (19).”
Background
Oncogenic Shp2 disturbs microtubule regulation to cause HDAC6-dependent ERK hyperactivation
Tien, S. C., & Chang, Z.-F. (2013) · Oncogene · doi:10.1038/onc.2013.241 · Cited by 29
Disruption to schizophrenia-associated gene Fez1 in the hippocampus of HDAC11 knockout mice
Bryant, D., Landles, C., Papadopoulou, A. S., Benjamin, A. C., Duckworth, J. K., Rosahl, T. W., Benn, C., & Bates, G. P. (2017) · Scientific Reports · doi:10.1038/s41598-017-11630-1 · Cited by 27
HDAC6 regulates sensitivity to cell death in response to stress and post-stress recovery
Ryu, H.-W., Won, H.-R., Lee, D. H., & Kwon, S. H. (2017) · Cell Stress and Chaperones · doi:10.1007/s12192-017-0763-3 · Cited by 32
Self-citation
Histone deacetylase 6’s function in viral infection, innate immunity, and disease: latest advances
Qu, M., Zhang, H., Cheng, P., Wubshet, A. K., Yin, X., Wang, X., & Sun, Y. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1216548 · Cited by 24
“HDAC6 knockout mice exhibited abnormalities in bone homeostasis and immunological function (38).”
Background
Significance of Five-Membered Heterocycles in Human Histone Deacetylase Inhibitors
Frühauf, A., Behringer, M., & Meyer‐Almes, F. (2023) · Molecules · doi:10.3390/molecules28155686 · Cited by 36
“The great therapeutic window is supported by HDAC6 knock-out (KO) studies in mice, developing normally with no apparent phenotype [38].”
Background
ACY-241, an HDAC6 inhibitor, overcomes erlotinib resistance in human pancreatic cancer cells by inducing autophagy
Park, S., Joo, S. H., Lee, N., Jang, W., Seo, J. H., & Jeong, C. (2021) · Archives of Pharmacal Research · doi:10.1007/s12272-021-01359-x · Cited by 27

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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