Cited by 765Histone Deacetylase Inhibitors ResearchMicrotubule and mitosis dynamicsGenomics and Chromatin Dynamics

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HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo

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Zhang, Yu, Li, Na, Caron, Cécile, Matthias, Gabriele, Hess, Daniel, Khochbin, Saadi, Matthias, Patrick·2003·The EMBO Journal

DOI 10.1093/emboj/cdg115PMC PMC150348

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Abstract

Microtubules are cylindrical cytoskeletal structures found in almost all eukaryotic cell types which are involved in a great variety of cellular processes. Reversible acetylation on the epsilon-amino group of alpha-tubulin Lys40 marks stabilized microtubule structures and may contribute to regulating microtubule dynamics. Yet, the enzymes catalysing this acetylation/deacetylation have remained unidentified until recently. Here we report that beta-tubulin interacts with histone deacetylase-6 (HDAC-6) in a yeast two-hybrid assay and in vitro. We find that HDAC-6 is a micro tubule-associated protein capable of deacetylating alpha-tubulin in vivo and in vitro. HDAC-6's microtubule binding and deacetylation functions both depend on the hdac domains. Overexpression of HDAC-6 in mammalian cells leads to tubulin hypoacetylation. In contrast, inhibition of HDAC-6 function by two independent mechanisms--pharmacological (HDAC inhibitors) or genetic (targeted inactivation of HDAC-6 in embryonic stem cells)--leads to hyperacetylation of tubulin and microtubules. Taken together, our data provide evidence that HDAC-6 might act as a dual deacetylase for tubulin and histones, and suggest the possibility that acetylated non-histone proteins might represent novel targets for pharmacological therapy by HDAC inhibitors.

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Items 201–300 of 765

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“HDAC6 KO mice have no discernible phenotype beyond hyperacetylated tubulin (Hubbert et al., 2002; Zhang et al., 2003).”
Background
A microenvironment-mediated c-Myc/miR-548m/HDAC6 amplification loop in non-Hodgkin B cell lymphomas
Lwin, T., Zhao, X., Cheng, F., Zhang, X., Huang, A., Shah, B. D., Zhang, Y., Moscinski, L. C., Choi, Y. S., Kozikowski, A. P., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64210 · Cited by 75
“Given that tubastatin A has been shown to be a new, potentially antitumor drug (14–18), we also tested whether inhibition of HDAC6 by tubastatin A suppresses lymphoma cell colony formation and blocks stroma-medi-ated clonogenicity.”
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“In addition to their role in regulating chromatin structure and gene expression, HDACs deacetylate non-histone proteins such as p53 [1,2], Sp1 [3], E2F [4,5], cAMP response-element-binding protein (CREB) [6], GATA1 [7,8] and tubulin [9].”
Cytoplasmic Sequestration of HDAC7 from Mitochondrial and Nuclear Compartments upon Initiation of Apoptosis
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“Its acetylation at Lys40 is a marker of stabilized microtubules [41, 43, 162] and is regulated by HDAC6 [163].”
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Calfa, G. D., Chapleau, C. A., Campbell, S. L., Inoue, T., Morse, S. J., Lubin, F. D., & Pozzo‐Miller, L. D. (2011) · Hippocampus · doi:10.1002/hipo.20990 · Cited by 76
“In fact, alfa-tubulin is deacetylated in Lys-40 by HDAC6 in vitro and in vivo (Hubbert et al., 2002; Zhang et al., 2003; Dompierre et al., 2007), potentially affecting dynamic microtubules within dendritic spines (Gu et al., 2008; Jaworski et al., 2009).”
Background
F11L-Mediated Inhibition of RhoA-mDia Signaling Stimulates Microtubule Dynamics during Vaccinia Virus Infection
Arakawa, Y., Cordeiro, J. V., & Way, M. (2007) · Cell Host & Microbe · doi:10.1016/j.chom.2007.04.007 · Cited by 72
“Tubulin deacetylation is known to be dependent on the activity of HDAC6, which associates with microtubules and leads to a global deacetylationofa-tubulin (Hubbert et al., 2002;Matsuyamaet al., 2002; Zhang et al., 2003).”
Background
Role of tubulin acetylation in cellular functions and diseases
Nekooki-Machida, Y., & Hagiwara, H. (2020) · Medical Molecular Morphology · doi:10.1007/s00795-020-00260-8 · Cited by 74
Brain lesions comprised of aluminum-rich cells that lack microtubules may be associated with the cognitive deficit of Alzheimer's disease
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“(1) Anti-acetylated-atubulin antibody (clone 6-11B-1, Sigma–Aldrich) was diluted 1:500 and (2) neuron-specific anti-b-tubulin, C-terminal antibody (clone TU-20, Millipore) diluted 1:50, as markers for acetylated microtubules (Zhang et al., 2003) and non-acetylated microtubules, respectively.”
Method
Phase I study of vorinostat (suberoylanilide hydroxamic acid, NSC 701852) in combination with docetaxel in patients with advanced and relapsed solid malignancies
Schneider, B. J., Kalemkerian, G. P., Bradley, D., Smith, D. C., Egorin, M. J., Daignault, S. D., Dunn, R. L., & Hussain, M. (2010) · Investigational New Drugs · doi:10.1007/s10637-010-9503-6 · Cited by 71
“Also, HDAC 6 appears to be specific for de-acetylation of alpha tubulin [ 20 ].”
Background
HDAC6 Regulates Mutant SOD1 Aggregation through Two SMIR Motifs and Tubulin Acetylation
Gál, J., Chen, J., Barnett, K. R., Yang, L., Brumley, E., & Zhu, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.431957 · Cited by 70
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“This is also consistent with previous studies that identify class I HDACs as significantly differentially expressed in ATRT (33) rather than class II HDACs such as HDAC6 that have been found to modulate acetylation of a-tubulin (34).”
Result
Valproic acid inhibits proliferation of HER2-expressing breast cancer cells by inducing cell cycle arrest and apoptosis through Hsp70 acetylation
Mawatari, T., Ninomiya, I., Inokuchi, M., HARADA, S., Hayashi, H., Oyama, K., Makino, I., Nakagawara, H., Miyashita, T., Tajima, H., et al. (2015) · International Journal of Oncology · doi:10.3892/ijo.2015.3213 · Cited by 69
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Background
Recent Advances in Elucidating Paclitaxel Resistance Mechanisms in Non-small Cell Lung Cancer and Strategies to Overcome Drug Resistance
Cui, H., Arnst, K. E., Miller, D. D., & Li, W. (2020) · Current Medicinal Chemistry · doi:10.2174/0929867326666191016113631 · Cited by 71
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Class II HDAC Inhibition Hampers Hepatic Stellate Cell Activation by Induction of MicroRNA-29
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“The class IIb HDAC6 displays distinct functionality, as its inhibition stimulates tubulin acetylation and influences cell motility [20,21,22].”
Background
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Ren, Y., Su, X., Kong, L., Li, M., Zhao, X., Yu, N., & Kang, J. (2016) · Inflammation Research · doi:10.1007/s00011-016-0984-4 · Cited by 68
“Histone acetylation enzymes 8 (HDAC8) is expressed in the heart, lungs, liver and kidneys [7], is an essential factor in the cell survival and proliferation [8], and it also can regulate differentiation and contraction of the smooth muscles.”
BackgroundInfluential
Inhibition of histone deacetylase 6 (HDAC6) protects against vincristine-induced peripheral neuropathies and inhibits tumor growth
Helleputte, L. V., Kater, M. S. J., Cook, D. P., Eykens, C., Rossaert, E., Haeck, W., Jaspers, T., Geens, N., Berghe, P. V., Gysemans, C. A., et al. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.11.011 · Cited by 66
“These unique features allow HDAC6 to interact with substrates other than histones, including α-tubulin (Hubbert et al., 2002; Zhang et al., 2003).”
Systemic anti-vascular endothelial growth factor therapies induce a painful sensory neuropathy
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“Overall, this finding supports previous observations that hyperacetylation of -tubulin represents a marker rather than a cause of microtubule hyperstability (Zhang et al., 2003).”
Result
Actin-microtubule cytoskeletal interplay mediated by MRTF-A/SRF signaling promotes dilated cardiomyopathy caused by LMNA mutations
Dour, C. L., Chatzifrangkeskou, M., Macquart, C., Magiera, M. M., Peccate, C., Jouve, C., Virtanen, L., Heliö, T. M., Aalto‐Setälä, K., Crasto, S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-35639-x · Cited by 69
“…mutant A-type lamins SRF mediates the transcription of ATAT1 encoding α -tubulin acetyl-transferase 1 ( α -TAT1) 49 , which catalyzes the lysine (K)40 acetylation of α -tubulin 50,51 , which in turn is speci ﬁ cally deacetylated by histone deacetylase-6(HDAC6) 52,53 (schematicallyshowninFig.4a).”
Proteomic identification and functional characterization of MYH9, Hsc70, and DNAJA1 as novel substrates of HDAC6 deacetylase activity
Zhang, L., Liu, S., Liu, N., Zhang, Y., Liu, M., Li, D., Seto, E., Yao, T., Shui, W., & Zhou, J. (2014) · Protein & Cell · doi:10.1007/s13238-014-0102-8 · Cited by 66
“Previous studies havedocumented several proteins as the substrates of HDAC6, including α-tubulin (Hubbert et al., 2002; Zhang et al., 2003), Hsp90 (Kovacs et al.”
BackgroundInfluential
Subcellular Localization of Class II HDAs in Arabidopsis thaliana: Nucleocytoplasmic Shuttling of HDA15 Is Driven by Light
Alinsug, M. V., Chen, F. F., Luo, M., Tai, R., Jiang, L., & Wu, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030846 · Cited by 71
Characterisation of the in vitro activity of the depsipeptide histone deacetylase inhibitor spiruchostatin A
Crabb, S. J., Howell, M., Rogers, H. L., Ishfaq, M., Yurek‐George, A., Carey, K. L., Pickering, B. M., East, P., Mitter, R., Maeda, S., et al. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.06.004 · Cited by 66
“[8] Zhang Y, Li N, Caron C, Matthias G, Hess D, Khochbin S, et al.”
Background
Dissecting Histone Deacetylase 3 in Multiple Disease Conditions: Selective Inhibition as a Promising Therapeutic Strategy
Adhikari, N., Jha, T., & Ghosh, B. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01676 · Cited by 74
African swine fever virus-cell interactions: From virus entry to cell survival
Alonso, C., Galindo, I., Cuesta-Geijo, M. Á., Cabezas, M., Hernáez, B., & Muñoz-Moreno, R. (2012) · Virus Research · doi:10.1016/j.virusres.2012.12.006 · Cited by 66
A Tale of the Good and Bad: Remodeling of the Microtubule Network in the Brain by Cdk5
Shah, K., & Lahiri, D. K. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9792-7 · Cited by 71
“Mechanistically, α-tubulins are acetylated and deacetylated by histone acetyltransferases (HATs) and histone deacetylases (HDACs), respectively [38].”
HDAC6 promotes cell proliferation and confers resistance to gefitinib in lung adenocarcinoma
Wang, Z., TANG, F., Hu, P., Wang, Y., Gong, J., Sun, S., & Xie, C. (2016) · Oncology Reports · doi:10.3892/or.2016.4811 · Cited by 65
HDAC11 deficiency disrupts oncogene-induced hematopoiesis in myeloproliferative neoplasms
Yue, L., Sharma, V., Horvat, N. P., Akuffo, A. A., Beatty, M. S., Murdun, C., Colin, C., Billington, J. M. R., Goodheart, W. E., Sahakian, E., et al. (2020) · Blood · doi:10.1182/blood.2019895326 · Cited by 67
Microtubule acetylation dyshomeostasis in Parkinson’s disease
Naren, P., Khan, S. S., Tryphena, K. P., Vora, L. K., Srivastava, S., Singh, S. B., & Khatri, D. K. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00354-0 · Cited by 66
Bortezomib interacts synergistically with belinostat in human acute myeloid leukaemia and acute lymphoblastic leukaemia cells in association with perturbations in NF‐κB and Bim
Dai, Y., Chen, S., Wang, L., Pei, X.-Y., Kramer, L. B., Dent, P., & Grant, S. (2011) · British Journal of Haematology · doi:10.1111/j.1365-2141.2011.08591.x · Cited by 64
“For example, certain HDACIs, such as fatty acids (sodium butyrate), benzamides (MS-275), or romidepsin (depsipeptide/FK288), primarily inhibit class I HDACs (e.g. HDAC 1, 2, and 3), while others, such as tubacin, specifically target class II HDACs (e.g. HDAC6) (Haggarty et al, 2003).”
BackgroundInfluential
Hdac6 regulates Tip60-p400 function in stem cells
Chen, P. B., Hung, J., Hickman, T. L., Coles, A. H., Carey, J. F., Weng, Z., Feixia Chu, C., & Fazzio, T. G. (2013) · eLife · doi:10.7554/elife.01557 · Cited by 64
“Furthermore, Hdac6 KD ESCs had a small but reproducible decrease in proliferation rate, while Tip60 KD caused a somewhat more severe proliferation defect (Figure 7B), consistent with previous studies (Zhang et al., 2003; Fazzio et al., 2008a).”
BackgroundResult
Histone deacetylase inhibitors that target tubulin
Schemies, J., Sippl, W., & Jung, M. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.01.040 · Cited by 66
“One important example is a-tubulin, but not all subtypes function as tubulin deacetylases, only HDAC6 [8–10] and Sirt2 [11] are able to accept it as a substrate and control the level of tubulin acetylation which has an impact on the microtubule network.”
Background
Identification of novel modulators of mitochondrial function by a genome-wide RNAi screen in Drosophila melanogasterPreprint
Chen, J., Shi, X., Padmanabhan, R., Wang, Q., Wu, Z., Stevenson, S. C., Hild, M., Garza, D., & Li, H. (2007) · Genome Research · doi:10.1101/gr.6940108 · Cited by 65
Vorinostat, a histone deacetylase inhibitor, facilitates fear extinction and enhances expression of the hippocampal NR2B-containing NMDA receptor gene
Fujita, Y., Morinobu, S., Takei, S., Fuchikami, M., Matsumoto, T., Yamamoto, S., & Yamawaki, S. (2012) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2012.01.026 · Cited by 66
“In this context, the acetylation of non-histone cellular proteins may be involved in diverse biological functions via transcriptional-dependent (Yeh et al., 2004) as well as transcriptional-independent mechanisms (Bolden et al., 2006; Zhang et al., 2003).”
Background
RETRACTED: Synergistic Antitumor Effects of Novel HDAC Inhibitors and Paclitaxel In Vitro and In Vivo
Zuco, V., Cesare, M. D., Cincinelli, R., Nannei, R., Pisano, C., Zaffaroni, N., & Zunino, F. (2011) · PLoS ONE · doi:10.1371/journal.pone.0029085 · Cited by 63
“…p53), and by functional alterations of critical proteins (e.g., tubulin and Hsp90) [15,16,39] The latter effects, which involve the inhibition of the cytoplasmatically localized HDAC6 isoform [15,16,40,41], have been exploited to achieve a synergistic interaction between pan-HDACi and taxanes [21].”
Retracted
A selective histone deacetylase-6 inhibitor improves BDNF trafficking in hippocampal neurons from Mecp2 knockout mice: implications for Rett syndrome
Xu, X., Kozikowski, A. P., & Pozzo‐Miller, L. D. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00068 · Cited by 63
“A number of genes including brain-derived neurotrophic factor (Bdnf ) were identified to be regulated by MeCP2 and relevant to the pathogenesis of RTT (Bievenu and Chelly, 2006; Chahrour and Zoghbi, 2007).”
Background
Histone deacetylase 6 and cytoplasmic linker protein 170 function together to regulate the motility of pancreatic cancer cells
Li, D., Sun, X., Zhang, L., Yan, B., Xie, S., Liu, R., Liu, M., & Zhou, J. (2014) · Protein & Cell · doi:10.1007/s13238-013-0010-3 · Cited by 63
“HDAC6 has been shown to participate in a wide range of cellular processes primarily through its deacetylation of α-tubulin, the actin-binding protein cortactin, and the molecular chaperone heat shock protein 90 (Hubbert et al., 2002; Matsuyama et al., 2002; Zhang et al., 2003; Kovacs et al., 2005; Zhang et al., 2007).”
Targeted inhibition of histone deacetylase 6 in inflammatory diseases
Ran, J., & Zhou, J. (2019) · Thoracic Cancer · doi:10.1111/1759-7714.12974 · Cited by 63
Interplay between histone deacetylases and autophagy ‐ from cancer therapy to neurodegeneration
Truee, O., & Matthias, P. (2011) · Immunology and Cell Biology · doi:10.1038/icb.2011.103 · Cited by 64
Elongator – an emerging role in neurological disorders
Nguyen, L., Humbert, S., Saudou, F., & Chariot, A. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.11.002 · Cited by 61
Lysine deacetylases and mitochondrial dynamics in neurodegeneration
Guedes-Dias, P., & Oliveira, J. M. A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.005 · Cited by 63
“Conversely, two KDACs, specifically HDAC6 and SIRT2, were found to interact and deacetylate α-tubulin in vitro and in vivo [141–143] (Fig.”
Background
Kinetic Stabilization of Microtubule Dynamics by Estramustine Is Associated with Tubulin Acetylation, Spindle Abnormalities, and Mitotic Arrest
Mohan, R., & Panda, D. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0584 · Cited by 61
“Overexpression of both HDAC6 and SIRT2 are shown to destabilize microtubules (46, 47).”
Background
Selective HDAC6 inhibition prevents TNF-α-induced lung endothelial cell barrier disruption and endotoxin-induced pulmonary edema
Yu, J., Ma, Z., Shetty, S., Ma, M., & Fu, J. (2016) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00051.2016 · Cited by 61
“Indeed, acetylation of -tubulin is known to promote MT stability (40, 51).”
BackgroundInfluential
Antibodies Immobilized as Arrays to Profile Protein Post-translational Modifications in Mammalian Cells
Ivanov, S. S., Chung, A. S., Yuan, Z., Guan, Y. A., Sachs, K. V., Reichner, J. S., & Chin, Y. E. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m300130-mcp200 · Cited by 61
“TSA has been reported to induce strong -tubulin acetylation on lysine-40 residue within the N terminus (19).”
Background
Antiproliferative and proapoptotic activities of 4-hydroxybenzoic acid-based inhibitors of histone deacetylases
Seidel, C., Schnekenburger, M., Dicato, M. A., & Diederich, M. F. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.09.026 · Cited by 60
HDAC2 regulates chromatin plasticity and enhances DNA vulnerability
Marchion, D. C., Biçaku, E., Turner, J. G., Schmitt, M. L., Morelli, D., & Münster, P. N. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-0985 · Cited by 62
“However, several investigators have reported effects on nonhistone targets of HDAC6 (35, 36); therefore, we also evaluated the effects of HDAC6 depletion on epirubicin sensitivity.”
Background
HDAC6 regulates microtubule stability and clustering of AChRs at neuromuscular junctions
Osseni, A., Ravel‐Chapuis, A., Thomas, J.-L., Gache, V., Schaeffer, L., & Jasmin, B. J. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201901099 · Cited by 55
Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation
Carmona, B., Marinho, H. S., Matos, C. L., Nolasco, S., & Soares, H. (2023) · Biology · doi:10.3390/biology12040561 · Cited by 64
“Despite this interaction, HDAC6 and SIRT2 are able to individually catalyze the deacetylation of α-tubulin, in vitro and in vivo [148,204,206,231].”
Background
DFT-based ranking of zinc-binding groups in histone deacetylase inhibitors
Vanommeslaeghe, K., Loverix, S., Geerlings, P., & Tourwé, D. A. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.06.009 · Cited by 59
A phase I-II study of the histone deacetylase inhibitor vorinostat plus sequential weekly paclitaxel and doxorubicin-cyclophosphamide in locally advanced breast cancer
Tu, Y., Hershman, D. L., Bhalla, K. N., Fiskus, W. C., Pellegrino, C. M., Andreopoulou, E., Makower, D., Kalinsky, K. M., Fehn, K., Fineberg, S., et al. (2014) · Breast Cancer Research and Treatment · doi:10.1007/s10549-014-3008-5 · Cited by 59
“[2, 6, 7] Since AKT and c-Raf confer resistance to tubulin polymerizing agents, vorinostat-induced depletion of these proteins also sensitizes cells to taxanes.”
Background
Histone deacetylases (HDAC) in physiological and pathological bone remodelling
Cantley, M. D., Zannettino, A. C. W., Bartold, P. M., Fairlie, D. P., & Haynes, D. R. (2016) · Bone · doi:10.1016/j.bone.2016.11.028 · Cited by 63
“HDAC 6 is amainly cytoplasmic protein of class IIb HDACs that act on both histones and the cytoplasmic protein tubulin [53].”
Background
A Role for the Chaperone Complex BAG3-HSPB8 in Actin Dynamics, Spindle Orientation and Proper Chromosome Segregation during Mitosis
Fuchs, M., Luthold, C., Guilbert, S. M., Varlet, A., Lambert, H., Jetté, A., Elowe, S., Landry, J., & Lavoie, J. N. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005582 · Cited by 58
“Beyond its role in the segregation and aggresome-targeting of misfolded proteins, HDAC6 possesses several cytoskeletal substrates of relevance for remodeling of actin-based mitotic structures and spindle orientation, including the actin-binding protein cortactin and a-tubulin [73, 74].”
Background
Selective class IIa HDAC inhibitors: myth or reality
Giorgio, E. D., Gagliostro, E., & Brancolini, C. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1727-8 · Cited by 62
“Concerning the latter point, the increase in the acetylation of tubulin is probably due to the targeting of HDAC6 [78] and seems to be unrelated to the suppression of class IIa”
Background
HDACs class II-selective inhibition alters nuclear receptor-dependent differentiation
Nebbioso, A., Dell’Aversana, C., Bugge, A. K., Sarno, R., Valente, S., Rotili, D., Manzo, F., Teti, D. V., Mandrup, S., Ciana, P., et al. (2010) · Journal of Molecular Endocrinology · doi:10.1677/jme-10-0043 · Cited by 59
Microtubules are more stable and more highly acetylated in ethanol-treated hepatic cells
Kannarkat, G. T., Tuma, D. J., & Tuma, P. L. (2005) · Journal of Hepatology · doi:10.1016/j.jhep.2005.07.007 · Cited by 58
“In contrast, when the enzymes are inactivated by pharmacological agents or their expression is knocked down, microtubules are more stable and hyperacetylated up to five-fold [28–31].”
Background
Oligodendrocyte process outgrowth in vitro is modulated by epigenetic regulation of cytoskeletal severing proteins
Liu, A., Muggironi, M., Marin‐Husstege, M., & Casaccia‐Bonnefil, P. (2003) · Glia · doi:10.1002/glia.10290 · Cited by 58
“It has been recently proposed that the effect of TSA on the morphology of tumor cell line is mediated by the inhibition of HDAC-6, which is responsible for deacetylation of -tubulin (Hubbert et al., 2002; Zhang et al., 2003).”
Background
Primary cilium: an elaborate structure that blocks cell division?
Ke, Y., & Yang, W. (2014) · Gene · doi:10.1016/j.gene.2014.06.050 · Cited by 64
“HDAC6 is not an essential protein in embryonic development since HDAC6 gene disruption does not obviously alter embryonic stem proliferation or embryo morphogenesis (Zhang et al., 2003).”
Background
Function of Sirtuins in Biological Tissues
Shoba, B., Lwin, Z. M., Ling, L. S., Bay, B., Yip, G. W. C., & Srinivasan, D. K. (2009) · The Anatomical Record · doi:10.1002/ar.20875 · Cited by 58
“SIRT2 mainly deacetylates a-tubulin, which co-localizes with microtubules and HDAC6 (Hubbert et al., 2002; North et al., 2003; Zhang et al., 2003).”
Background
Increased gene expression of histone deacetylases in patients with Philadelphia-negative chronic myeloproliferative neoplasms
Skov, V., Larsen, T. S., Thomassen, M., Riley, C. H., Jensen, M. K., Bjerrum, O. W., Kruse, T. A., & Hasselbalch, H. C. (2011) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2011.597905 · Cited by 57
Function of Drg1/Rit42 in p53-dependent Mitotic Spindle Checkpoint
Kim, K., Ongusaha, P. P., Hong, Y., Kurdistani, S. K., Nakamura, M., Lu, K. P., & Lee, S. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400781200 · Cited by 57
Direct Binding with Histone Deacetylase 6 Mediates the Reversible Recruitment of Parkin to the Centrosome
Jiang, Q., Ren, Y., & Feng, J. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2860-08.2008 · Cited by 59
“To provide more evidence, we transfected SHSY5Y cells with GFP and wild-type HDAC6 (wt-H6) or the catalytically inactive HDAC6 double mutant (mut-H6, H216A/H611A), which loses the ability to deacetylate tubulin (Zhang et al., 2003).”
Epigenetic considerations for endometrial cancer prevention, diagnosis and treatment
ZHOU, X., Dowdy, S. C., Podratz, K. C., & JIANG, S. (2007) · Gynecologic Oncology · doi:10.1016/j.ygyno.2007.06.019 · Cited by 56
c-Cbl and Cbl-b Act Redundantly to Protect Osteoclasts from Apoptosis and to Displace HDAC6 from β-Tubulin, Stabilizing Microtubules and Podosomes
Purev, E., Neff, L., Horne, W. C., & Baron, R. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-03-0248 · Cited by 59
“Because both c-Cbl and HDAC6 bind tubulin (Zhang et al., 2003; Teckchandani et al., 2005), Cbl proteins might antagonize HDAC6-catalyzed microtubule deacetylation by competitively displacing HDAC6 from the MTs.”
Background
Uropathogenic Escherichia coli Invades Host Cells via an HDAC6-modulated Microtubule-dependent Pathway
Dhakal, B. K., & Mulvey, M. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805010200 · Cited by 56
IKAP/Elp1 involvement in cytoskeleton regulation and implication for familial dysautonomia
Cheishvili, D., Maayan, C., Cohen-Kupiec, R., Lefler, S., Weil, M., Ast, G., & Razin, A. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr036 · Cited by 56
Microtubule Dynamic Instability Controls Podosome Patterning in Osteoclasts through EB1, Cortactin, and Src
Duplan, M. B., Zalli, D., Stephens, S., Zenger, S., Neff, L., Oelkers, J. M., Lai, F. P. L., Horne, W. C., Rottner, K., & Baron, R. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00578-13 · Cited by 59
“DMSO or sodium butyrate (NaB), a deacetylase inhibitor that does not affect -tubulin acetylation (48), was used as a control.”
Method
Son maintains accurate splicing for a subset of human pre-mRNAs
Sharma, A., Markey, M. P., Torres-Munoz, K. N., Varia, S. N., Kadakia, M., Bubulya, A., & Bubulya, P. A. (2011) · Journal of Cell Science · doi:10.1242/jcs.092239 · Cited by 56
“HDAC6 not only deacetylates histone tails to regulate gene expression (Narlikar et al., 2002), but it also deacetylates tubulin at Lys40 and thereby influences the stability of the microtubule network (Zhang et al., 2003; Zhao et al., 2010).”
Background
HDAC6 Inhibitors Rescued the Defective Axonal Mitochondrial Movement in Motor Neurons Derived from the Induced Pluripotent Stem Cells of Peripheral Neuropathy Patients with HSPB1 Mutation
Kim, J. Y., Woo, S., Hong, Y. B., Choi, H., Kim, J., Choi, H., Mook‐Jung, I., Ha, N., Kyung, J., Koo, S. K., et al. (2016) · Stem Cells International · doi:10.1155/2016/9475981 · Cited by 56
“Histone deacetylase 6 (HDAC6) is a class IIb HDAC that regulates acetylation states of 𝛼 -tubulin [8, 9].”
Microtubules in Influenza Virus Entry and Egress
Simpson, C., & Yamauchi, Y. (2020) · Viruses · doi:10.3390/v12010117 · Cited by 57
Requirement of histone deacetylase activity for the expression of critical photoreceptor genes
Chen, B., & Cepko, C. L. (2007) · BMC Developmental Biology · doi:10.1186/1471-213x-7-78 · Cited by 56
“Other non-histone HDAC substrates include transcription factors, such as E2F1, MyoD, GATA-1, and p53 [5-9], as well as proteins in the cytoplasm, such as tubulin and hsp90 [10-14].”
Background
Epigenetic Drugs for Cancer and microRNAs: A Focus on Histone Deacetylase Inhibitors
Autin, P., Blanquart, C., & Fradin, D. (2019) · Cancers · doi:10.3390/cancers11101530 · Cited by 56
The HDAC Inhibitor LBH589 Induces ERK-Dependent Prometaphase Arrest in Prostate Cancer via HDAC6 Inactivation and Down-Regulation
Chuang, M., Wu, S.-T., Tang, S., Lai, X., Lai, H.-C., Hsu, K.-H., Sun, K., Sun, G.-H., Chang, S.-Y., Yü, D., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073401 · Cited by 54
“HDAC6 is the major deacetylase that is responsible for deacetylation of α-tubulin and HSP90 to modulate microtubulin-dependent transportation, recruit misfolded proteins, and transport to aggresomes for degradation [27–29].”
Background
LC3B-II deacetylation by histone deacetylase 6 is involved in serum-starvation-induced autophagic degradation
Liu, K., Zhou, D., Ouyang, D., Xu, L., Wang, Y., Wang, L., Pan, H., & He, X. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.11.007 · Cited by 56
Trichostatin A prevents neointimal hyperplasia via activation of Krüppel like factor 4
Kee, H. J., Kwon, J., Shin, S., Ahn, Y., Jeong, M. H., & Kook, H. (2011) · Vascular Pharmacology · doi:10.1016/j.vph.2011.07.001 · Cited by 55
“Although HDACs can deacetylate histones, recent reports have shown that HDACsmay target many nonhistone proteins as well, such as a-tubulin, GATA4, p53, YY1, MEF2D, hsp90, and E2F1 (Gregoire et al., 2007; North et al., 2003; Yao et al., 2001; Zhang et al., 2003).”
Background
Regulation of adipogenesis by cytoskeleton remodelling is facilitated by acetyltransferase MEC-17-dependent acetylation of α-tubulin
Yang, W., Guo, X., Thein, S., Xu, F., Sugii, S., Baas, P. W., Radda, G. K., & Han, W. (2012) · Biochemical Journal · doi:10.1042/bj20121121 · Cited by 54
Histone deacetylase 6 gates the synaptic action of acute stress in prefrontal cortex
Lee, J. B., Wei, J., Liu, W., Cheng, J., Feng, J., & Yan, Z. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2011.224907 · Cited by 52
“For instance, the deacetylation of tublin by HDAC6 (Hubbert et al. 2002; Zhang et al. 2003) causes the recruitment of molecular motors dynein and kinesin-1 to microtubules, which influences the vesicular transport of BDNF (Dompierre et al. 2007).”
Background
Selective inhibition of histone deacetylase 3 by novel hydrazide based small molecules as therapeutic intervention for the treatment of cancer
Pulya, S., Patel, T. K., Paul, M., Adhikari, N., Banerjee, S., Routholla, G., Biswas, S., Jha, T., & Ghosh, B. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114470 · Cited by 55
Microtubule-Associated Histone Deacetylase 6 Supports the Calcium Store Sensor STIM1 in Mediating Malignant Cell Behaviors
Chen, Y., Chen, Y., Chiu, W., Liu, K.-Y., Liu, Y.-L., Chang, J., Chang, H., & Shen, M. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-4127 · Cited by 53
Nuclear HDAC6 inhibits invasion by suppressing NF-κB/MMP2 and is inversely correlated with metastasis of non-small cell lung cancer
Yang, C., Liu, Y.-P., Dai, H.-Y., Shiue, Y., Tsai, C.-J., Huang, M., & Yeh, Y. (2015) · Oncotarget · doi:10.18632/oncotarget.4749 · Cited by 53
“It has been revealed that HDAC6 contributes to the deacetylation of α-tubulin and enhances cell mobility [22].”
Background
The growing landscape of tubulin acetylation: lysine 40 and many more
Sadoul, K., & Khochbin, S. (2016) · Biochemical Journal · doi:10.1042/bcj20160172 · Cited by 53
Ricolinostat, a selective HDAC6 inhibitor, shows anti-lymphoma cell activity alone and in combination with bendamustine
Cosenza, M., Civallero, M., Marcheselli, L., Sacchi, S., & Pozzi, S. (2017) · APOPTOSIS · doi:10.1007/s10495-017-1364-4 · Cited by 52
“The inhibition of HDAC6 function leads to acetylation of tubulin and microtubules and thus stabilizes microtubule [48].”
Background
Targeting HDAC Complexes in Asthma and COPD
Zwinderman, M. R. H., de Weerd, S., & Dekker, F. J. (2019) · Epigenomes · doi:10.3390/epigenomes3030019 · Cited by 52
“Tubulin is a major component of the cytoskeleton and is thereby involved in cell motility [85,86].”
Background
The B′ Protein Phosphatase 2A Regulatory Subunit well-rounded Regulates Synaptic Growth and Cytoskeletal Stability at the Drosophila Neuromuscular Junction
Viquez, N. M., Li, C. R., Wairkar, Y. P., & DiAntonio, A. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1740-06.2006 · Cited by 53
“As a second measure of microtubule organization, we stained for acetylated tubulin, a marker of stabilized microtubules (Zhang et al., 2003).”
Background
Effects of valproic acid on the cell cycle and apoptosis through acetylation of histone and tubulin in a scirrhous gastric cancer cell line
Yagi, Y., Fushida, S., Harada, S., Kinoshita, J., Makino, I., Oyama, K., Tajima, H., Fujita, H., Takamura, H., Ninomiya, I., et al. (2010) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/1756-9966-29-149 · Cited by 53
“Interestingly, tubulin acetylation has a direct relation with HDAC6 inhibition induced by the action of VPA [42,43].”
Background
p97/valosin‐containing protein (VCP) is highly modulated by phosphorylation and acetylation
Konya, C., Kato, N., Maeda, R., Yasuda, K., Higashimae, N., Noguchi, M., Koike, M., Kimura, Y., Ohizumi, H., Hori, S., et al. (2009) · Genes to Cells · doi:10.1111/j.1365-2443.2009.01286.x · Cited by 51
“Interestingly, acetylated α-tubulin has been shown to be deacetylated by HDAC6 (Hubbert et al. 2002; Matsuyama et al. 2002; Zhang et al. 2003), and HDAC6 and VCP have been reported to physically interact each other (SeigneurinBerny et al. 2001).”
Background
HDAC6: Physiological function and its selective inhibitors for cancer treatment
Yang, P. (2013) · Drug Discoveries & Therapeutics · doi:10.5582/ddt.2013.v7.6.233 · Cited by 56
“To date, only HDAC6 (5-7) and Sirt2 (8) can use tubulin as a substrate and regulate the balance of tubulin acetylation and deacetylation.”
Background
Critical role of the HDAC6–cortactin axis in human megakaryocyte maturation leading to a proplatelet-formation defect
Messaoudi, K., Ali, A., Ishaq, R., Palazzo, A., Sliwa, D., Bluteau, O., Souquère, S., Muller, D., Diop, M. K., Rameau, P., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01690-2 · Cited by 52
Novel spiroindoline HDAC inhibitors: Synthesis, molecular modelling and biological studies
Brindisi, M., Senger, J., Cavella, C., Grillo, A., Chemi, G., Gemma, S., Cucinella, D. M., Lamponi, S., Sarno, F., Iside, C., et al. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.07.069 · Cited by 54
A New Amidohydrolase from Bordetella or Alcaligenes Strain FB188 with Similarities to Histone Deacetylases
Hildmann, C., Ninković, M., Dietrich, R., Wegener, D., Riester, D., Zimmermann, T. P., Birch, O. M., Bernegger, C., Loidl, P., & Schwienhorst, A. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.8.2328-2339.2004 · Cited by 52
“The closest homolog among human HDACs is HDAC6, a presumptive tubulin deacetylase (12).”
Influential
Development of HDAC Inhibitors Exhibiting Therapeutic Potential in T-Cell Prolymphocytic Leukemia
Toutah, K., Nawar, N., Timonen, S., Sorger, H., Raouf, Y. S., Bukhari, S., von Jan, J., Ianevski, A., Gawel, J. M., Olaoye, O. O., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00420 · Cited by 51
“11,12,14 In the past two decades, successful e ﬀ orts have led to four HDACi receiving U.S. Food and Drug Administration (FDA) approval for hematological cancers: vorinostat (SAHA, a ), romidepsin (FK-228, b ), belinostat (PXD-101, c ), and panobinostat (LBH-589, d ), with several in clinical…”
Hyperforin and aristoforin inhibit lymphatic endothelial cell proliferation in vitro and suppress tumor‐induced lymphangiogenesis in vivo
Rothley, M., Schmid, A., Thiele, W., Schacht, V., Plaumann, D., Gärtner, M., Yektaoğlu, A., Bruyére, F., Noël, A., Giannis, A., et al. (2009) · International Journal of Cancer · doi:10.1002/ijc.24295 · Cited by 51
Histone Deacetylase 6 Represents a Novel Drug Target in the Oncogenic Hedgehog Signaling Pathway
Dhanyamraju, P. K., Holz, P. S., Finkernagel, F., Fendrich, V., & Lauth, M. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0481 · Cited by 53
“One of the most prominent and best characterized protein substrate is the a-subunit of tubulin (8, 50), throughwhich the enzyme regulatesmicrotubule dynamics and vesicular transport (51–53).”
Background
Synthesis and biological testing of novel pyridoisothiazolones as histone acetyltransferase inhibitors
Furdas, S. D., Shekfeh, S., Bissinger, E.-M., Wagner, J. M., Schlimme, S., Valkov, V., Hendzel, M. J., Jung, M., & Sippl, W. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.01.063 · Cited by 50
Histone deacetylase inhibitor‐mediated cell death is distinct from its global effect on chromatin
Luchenko, V. L., Litman, T., Chakraborty, A. R., Heffner, A., Devor, C. B., Wilkerson, J., Stein, W. D., Robey, R. W., Bangiolo, L., Levens, D., et al. (2014) · Molecular Oncology · doi:10.1016/j.molonc.2014.05.001 · Cited by 50
“It known that romidepsin has a relatively lower potency against HDAC6, which acetylates non-histone proteins such as a-tubulin, b-catenin, Hsp90 and others (Crabb et al., 2008; Robey et al., 2011; Zhang et al., 2003).”
Background
Histone deacetylase inhibition in the treatment of heart disease
Berry, J. M., Cao, D. J., Rothermel, B. A., & Hill, J. A. (2008) · Expert Opinion on Drug Safety · doi:10.1517/14740338.7.1.53 · Cited by 49
“• HDAC6 interacts with and deacetylates α -tubulin and microtubules [86,101] .”
Background
A Class 1 Histone Deacetylase with Potential as an Antifungal Target
Bauer, I., Varadarajan, D., Pidroni, A., Gross, S., Vergeiner, S., Faber, B., Hermann, M., Tribus, M., Brosch, G., & Graessle, S. (2016) · mBio · doi:10.1128/mbio.00831-16 · Cited by 49
“In concert with other modiﬁcations, however, not only does acetylation act as a speciﬁc signal for the recruitment of distinct transcription factors (10–12), but in fact, those factors themselves might be substrates of HATs and HDACs (13–15).”
Clostridium difficile Toxin A Decreases Acetylation of Tubulin, Leading to Microtubule Depolymerization through Activation of Histone Deacetylase 6, and This Mediates Acute Inflammation
Nam, H. J., Kang, J. K., Kim, S.-K., Ahn, K. J., Seok, H., Park, S. J., Chang, J., Pothoulakis, C., LaMont, J. T., & Kim, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.162743 · Cited by 49
Carbamazepine promotes Her-2 protein degradation in breast cancer cells by modulating HDAC6 activity and acetylation of Hsp90
Meng, Q., Chen, X., Sun, L., Zhao, C., Sui, G., & Cai, L. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0651-y · Cited by 48
“Some recent reports have demonstrated that HDAC6 is responsible for the deacetylation of acetyl-a-tubulin and acetyl-Hsp90 [14, 15].”
Background
New HDAC6-mediated deacetylation sites of tubulin in the mouse brain identified by quantitative mass spectrometry
Liu, N., Xiong, Y., Li, S., Ren, Y., He, Q., Gao, S., Zhou, J., & Shui, W. (2015) · Scientific Reports · doi:10.1038/srep16869 · Cited by 48

Authors: Zhang, Y., Li, N., Caron, C., Matthias, G., Hess, D., Khochbin, S., & Matthias, P.
Affiliations: Friedrich Miescher Institute (CH)
Inserm (FR)
Corresponding author: Matthias, Patrick
ORCID: Zhang, Yu
Li, Na
Matthias, Gabriele
Hess, Daniel
Khochbin, Saadi
Matthias, Patrick
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2003-03-03
Volume: 22
Issue: 5
Pages: 1168-1179
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1093/emboj/cdg115
PMC: PMC150348
OpenAlex: W1979832500
Cited by: 740
References: 38
Citations by year: 2026: 26 · 2025: 20 · 2024: 27 · 2023: 37 · 2022: 24 · 2021: 29 · 2020: 35 · 2019: 29 · 2018: 32 · 2017: 22 · 2016: 39 · 2015: 35 · 2014: 26 · 2013: 45 · 2012: 41
FWCI: 9.19
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Harvard University
University of California, San Francisco
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: histone deacetylase, tubulin deacetylation, alpha-tubulin, beta-tubulin, microtubules, tubulin acetylation, microtubule dynamics, histone deacetylase inhibitors, non-histone protein acetylation, cytoskeleton
MeSH terms: Histone Deacetylase 6, Acetylation, Animals, Cattle, Chromatography, High Pressure Liquid, Embryo, Mammalian, Histone Deacetylases, Humans, Kidney, Microtubules, Peptides, Protein Binding, Stem Cells, Tubulin, 3T3 Cells, Paclitaxel, Protein Structure, Tertiary, Two-Hybrid System Techniques, Mice

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HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo

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