Cited by 741Histone Deacetylase Inhibitors ResearchMicrotubule and mitosis dynamicsGenomics and Chromatin Dynamics

The DOI matches its Crossref record; 43 of the 45 references it cites were found in a registry or an index.

In vivo destabilization of dynamic microtubules by HDAC6‐mediated deacetylation

Open access

Matsuyama, Akihisa, Shimazu, Tadahiro, Sumida, Yuko, Saito, Akiko, Yoshimatsu, Yasuhiro, Seigneurin‐Berny, Daphné, Osada, Hiroyuki, Komatsu, Yasuhiko, Nishino, Norikazu, Khochbin, Saadi, Horinouchi, Sueharu, Yoshida, Minoru·2002·The EMBO Journal

DOI 10.1093/emboj/cdf682PMC PMC139102

Open this paper in CoChat — free account Open PDF

Abstract

Trichostatin A (TSA) inhibits all histone deacetylases (HDACs) of both class I and II, whereas trapoxin (TPX) cannot inhibit HDAC6, a cytoplasmic member of class II HDACs. We took advantage of this differential sensitivity of HDAC6 to TSA and TPX to identify its substrates. Using this approach, alpha-tubulin was identified as an HDAC6 substrate. HDAC6 deacetylated alpha-tubulin both in vivo and in vitro. Our investigations suggest that HDAC6 controls the stability of a dynamic pool of microtubules. Indeed, we found that highly acetylated microtubules observed after TSA treatment exhibited delayed drug-induced depolymerization and that HDAC6 overexpression prompted their induced depolymerization. Depolymerized tubulin was rapidly deacetylated in vivo, whereas tubulin acetylation occurred only after polymerization. We therefore suggest that acetylation and deacetylation are coupled to the microtubule turnover and that HDAC6 plays a key regulatory role in the stability of the dynamic microtubules.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1093/emboj/cdf682

Cites

43 of 43 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510
Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559
Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A.
Yoshida, M., Kijima, M., Akita, M., & Beppu, T. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44885-x · Cited by 1,856
Self-citation
Acetylation of Histones and Transcription-Related Factors
Sterner, D. E., & Berger, S. L. (2000) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.64.2.435-459.2000 · Cited by 1,824
High-Resolution Model of the Microtubule
Nogales, E., Whittaker, M., Milligan, R. A., & Downing, K. H. (1999) · Cell · doi:10.1016/s0092-8674(00)80961-7 · Cited by 1,200
Acetylation: a regulatory modification to rival phosphorylation?
Kouzarides, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.6.1176 · Cited by 1,155
Signaling to Chromatin through Histone Modifications
Cheung, P., Allis, C. D., & Sassone-Corsi, P. (2000) · Cell · doi:10.1016/s0092-8674(00)00118-5 · Cited by 989
A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases
Richon, V. M., Emiliani, S., Verdin, E., Webb, Y., Breslow, R., Rifkind, R. A., & Marks, P. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.3003 · Cited by 914
Microtubules containing acetylated alpha-tubulin in mammalian cells in culture.
Piperno, G., LeDizet, M., & Chang, X. J. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.2.289 · Cited by 873

Flagged first, then by citations

Show all 45 references

2 of the 45 references couldn’t be matched to a known paper.

Sorted by citations

Items 301–400 of 741

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
The disordered N-terminus of HDAC6 is a microtubule-binding domain critical for efficient tubulin deacetylation
Ustinova, K., Nováková, Z., Saito, M., Meleshin, M., Mikesova, J., Kutil, Z., Baranová, P., Havlínová, B., Schutkowski, M., Matthias, P., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011243 · Cited by 48
Metabolism, cytoskeleton and cellular signalling in the grip of protein Nϵ ‐ and O‐acetylation
Yang, X., & Grégoire, S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7400977 · Cited by 49
DIDO as a Switchboard that Regulates Self-Renewal and Differentiation in Embryonic Stem Cells
Fütterer, A., de Celis, J., Navajas, R., Almonacid, L., Gutiérrez, J., Gutiérrez, A., Pacios-Bras, C., Bernascone, I., Martín‐Belmonte, F., & Martínez‐A, C. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.02.013 · Cited by 45
Epigenetics Modifications and Therapeutic Prospects in Human Thyroid Cancer
Catalano, M. G., Fortunati, N., & Boccuzzi, G. (2012) · Frontiers in Endocrinology · doi:10.3389/fendo.2012.00040 · Cited by 50
BAG3 Pro209 mutants associated with myopathy and neuropathy relocate chaperones of the CASA-complex to aggresomes
Adriaenssens, E., Tedesco, B., Mediani, L., Asselbergh, B., Crippa, V., Antoniani, F., Carra, S., Poletti, A., & Timmerman, V. (2020) · Scientific Reports · doi:10.1038/s41598-020-65664-z · Cited by 47
Protein lysine acetylation in normal and leukaemic haematopoiesis: HDACs as possible therapeutic targets in adult AML
Bruserud, Ø., Stapnes, C., Tronstad, K. J., Ryningen, A., Ånensen, N., & Gjertsen, B. T. (2006) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.10.1.51 · Cited by 48
Chromatin Modifications as Targets for New Anticancer Drugs
Schäfer, S., & Jung, M. (2005) · Archiv der Pharmazie · doi:10.1002/ardp.200500984 · Cited by 47
Polarity Regulation in Migrating Neurons in the Cortex
Reiner, O., & Sapir, T. (2009) · Molecular Neurobiology · doi:10.1007/s12035-009-8065-0 · Cited by 48
Microtubules as a potential platform for energy transfer in biological systems: a target for implementing individualized, dynamic variability patterns to improve organ function
Ilan, Y. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04513-1 · Cited by 48
Tubulin must be acetylated in order to form a complex with membrane Na+,K+-ATPase and to inhibit its enzyme activity
Santander, V. S., Bisig, C. G., Purro, S. A., Casale, C. H., Arce, C. A., & Barra, H. S. (2006) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-006-9212-9 · Cited by 46
Emerging molecular therapies of advanced thyroid cancer
Catalano, M. G., Poli, R., Pugliese, M., Fortunati, N., & Boccuzzi, G. (2010) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2010.02.006 · Cited by 47
KD5170, a novel mercaptoketone-based histone deacetylase inhibitor that exhibits broad spectrum antitumor activity in vitro and in vivo
Hassig, C. A., Symons, K. T., Guo, X., Nguyen, P.-M., Annable, T., Wash, P. L., Payne, J. E., Jenkins, D. A., Bonnefous, C., Trotter, C., et al. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-2347 · Cited by 44
Ciliopathies: Does HDAC6 Represent a New Therapeutic Target?
Yu, F. D., Ran, J., & Zhou, J. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.11.002 · Cited by 45
Acquired vorinostat resistance shows partial cross-resistance to ‘second-generation’ HDAC inhibitors and correlates with loss of histone acetylation and apoptosis but not with altered HDAC and HAT activities
Dedes, K. J., Dedes, I., Imesch, P., von Bueren, A. O., Fink, D. A., & Fedier, A. (2009) · Anti-Cancer Drugs · doi:10.1097/cad.0b013e3283262a32 · Cited by 45
Centrosome and microtubule functions and dysfunctions in meiosis: implications for age-related infertility and developmental disorders
Schatten, H., & Sun, Q. (2015) · Reproduction Fertility and Development · doi:10.1071/rd14493 · Cited by 44
HDAC6 Suppresses Age-Dependent Ectopic Fat Accumulation by Maintaining the Proteostasis of PLIN2 in Drosophila
Yan, Y., Wang, H., Hu, M., Jiang, L., Wang, Y., Liu, P., Liang, X., Liu, J., Li, C., Battle, A. L., et al. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.09.001 · Cited by 45
Microtubule polyglutamylation and acetylation drive microtubule dynamics critical for platelet formation
van Dijk, J., Bompard, G., Cau, J., Kunishima, S., Rabeharivelo, G., Langerak, J. M., Cazevieille, C., Cavelier, P., Boizet‐Bonhoure, B., Delsert, C., et al. (2018) · BMC Biology · doi:10.1186/s12915-018-0584-6 · Cited by 44
How Influenza Virus Uses Host Cell Pathways during Uncoating
Moreira, É. A., Yamauchi, Y., & Matthias, P. (2021) · Cells · doi:10.3390/cells10071722 · Cited by 44
Preclinical validation of AR42, a novel histone deacetylase inhibitor, as treatment for vestibular schwannomas
Jacob, A., Oblinger, J. L., Bush, M. L., Brendel, V. J., Santarelli, G. D., Chaudhury, A. R., Kulp, S. K., Perle, K. M. D. L., Chen, C., Chang, L., et al. (2011) · The Laryngoscope · doi:10.1002/lary.22392 · Cited by 43
Concurrent opposite effects of trichostatin A, an inhibitor of histone deacetylases, on expression of α-MHC and cardiac tubulins: implication for gain in cardiac muscle contractility
Davis, F. J., Pillai, J. B., Gupta, M., & Gupta, M. P. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00789.2004 · Cited by 44
Tubacin Kills Epstein-Barr Virus (EBV)-Burkitt Lymphoma Cells by Inducing Reactive Oxygen Species and EBV Lymphoblastoid Cells by Inducing Apoptosis
Kawada, J., Zou, P., Mazitschek, R., Bradner, J. E., & Cohen, J. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809090200 · Cited by 43
SIRT2 inactivation reveals a subset of hyperacetylated perinuclear microtubules inaccessible to HDAC6
Skoge, R. H., & Ziegler, M. (2016) · Journal of Cell Science · doi:10.1242/jcs.187518 · Cited by 43
Small Molecule Antagonists of the Interaction between the Histone Deacetylase 6 Zinc-Finger Domain and Ubiquitin
Harding, R., de Freitas, R. F., Collins, P. M., Franzoni, I., Ravichandran, M., Ouyang, H., Juárez‐Ornelas, K. A., Lautens, M., Schapira, M., von Delft, F., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00933 · Cited by 41
Exercise Training and Epigenetic Regulation: Multilevel Modification and Regulation of Gene Expression
Soci, Ú. P. R., Melo, S. F. S., Gomes, J. L. P., Silveira, A. C., Nóbrega, C., & de Oliveira, E. M. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-4304-8_16 · Cited by 45
Selective Histone Deacetylase 6 Inhibition Normalizes B Cell Activation and Germinal Center Formation in a Model of Systemic Lupus Erythematosus
Ren, J., Catalina, M. D., Eden, K. B., Liao, X., Read, K. A., Luo, X., McMillan, R. P., Hulver, M. W., Jarpe, M. B., Bachali, P., et al. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02512 · Cited by 42
Class II-selective histone deacetylase inhibitors. Part 2: Alignment-independent GRIND 3-D QSAR, homology and docking studies
Ragno, R., Simeoni, S., Rotili, D., Caroli, A., Botta, G., Brosch, G., Massa, S., & Mai, A. (2007) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2007.05.004 · Cited by 41
Identification of Inhibitor Binding Site in Human Sirtuin 2 Using Molecular Docking and Dynamics Simulations
Sakkiah, S., Arooj, M., Kumar, M. R., Eom, S. H., & Lee, K. W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0051429 · Cited by 40
Protein Quality Control Activation and Microtubule Remodeling in Hypertrophic Cardiomyopathy
Dorsch, L. M., Schuldt, M., dos Remedios, C. G., Schinkel, A. F. L., de Jong, P. L., Michels, M., Kuster, D. W. D., Brundel, B. J. J. M., & van der Velden, J. (2019) · Cells · doi:10.3390/cells8070741 · Cited by 40
Microtubule acetylation and stability may explain alcohol-induced alterations in hepatic protein trafficking
Joseph, R. A., Shepard, B. D., Kannarkat, G. T., Rutledge, T. W., Tuma, D. J., & Tuma, P. L. (2007) · Hepatology · doi:10.1002/hep.22014 · Cited by 40
Design and Synthesis of a Potent Histone Deacetylase Inhibitor
Liu, T., Kapustin, G. V., & Etzkorn, F. A. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm061082q · Cited by 40
Structural and functional implications of phosphorylation and acetylation in the regulation of the AAA+ protein p97This paper is one of a selection of papers published in this special issue entitled 8th International Conference on AAA Proteins and has undergone the Journal's usual peer review process.
Ewens, C. A., Kloppsteck, P., Förster, A., Zhang, X., & Freemont, P. S. (2010) · Biochemistry and Cell Biology · doi:10.1139/o09-128 · Cited by 39
Class II and IV HDACs function as inhibitors of osteoclast differentiation
Blixt, N. C., Faulkner, B., Astleford, K., Lelich, R., Schering, J., Spencer, E., Gopalakrishnan, R., Jensen, E. D., & Mansky, K. C. (2017) · PLoS ONE · doi:10.1371/journal.pone.0185441 · Cited by 41
HDAC6 regulates lipid droplet turnover in response to nutrient deprivation via p62-mediated selective autophagy
Yan, Y., Wang, H., Wei, C., Xiang, Y., Liang, X., Phang, C.-W., & Jiao, R. (2019) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2019.03.008 · Cited by 40
Epigenetic Regulation of Multidrug Resistance Protein 1 and Breast Cancer Resistance Protein Transporters by Histone Deacetylase Inhibition
You, D., Richardson, J. R., & Aleksunes, L. M. (2020) · Drug Metabolism and Disposition · doi:10.1124/dmd.119.089953 · Cited by 40
Direct and indirect effects of tubulin post-translational modifications on microtubule stability: Insights and regulations
Bär, J., Popp, Y., Bucher, M., & Mikhaylova, M. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119241 · Cited by 40
Identification of the Ankyrin Repeat Proteins ANKRA and RFXANK as Novel Partners of Class IIa Histone Deacetylases
Wang, A. H., Grégoire, S., Zika, E., Xiao, L., Li, C. S., Li, H., Wright, K. L., Ting, J. P. ‐., & Yang, X. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500295200 · Cited by 39
Involvement of the SMRT/NCoR–HDAC3 complex in transcriptional repression by the CNOT2 subunit of the human Ccr4–Not complex
Jayne, S., Zwartjes, C. G. M., van Schaik, F. M. A., & Timmers, H. T. M. (2006) · Biochemical Journal · doi:10.1042/bj20060406 · Cited by 45
Histone deacetylase inhibitors modulate miRNA and mRNA expression, block metaphase, and induce apoptosis in inflammatory breast cancer cells
Chatterjee, N., Wang, W. W., Conklin, T., Chittur, S. V., & Tenniswood, M. (2013) · Cancer Biology & Therapy · doi:10.4161/cbt.25088 · Cited by 38
Synthesis and evaluation of aliphatic-chain hydroxamates capped with osthole derivatives as histone deacetylase inhibitors
Huang, W., Chen, C., Chao, S.-W., Yu, C.-C., Yang, C., Guh, J., Lin, Y.-C., Kuo, C.-I., Yang, P., & Chang, C.-I. (2011) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2011.06.002 · Cited by 37
Cellular defence or viral assist: the dilemma of HDAC6
Zheng, K., Jiang, Y., He, Z., Kitazato, K., & Wang, Y. (2016) · Journal of General Virology · doi:10.1099/jgv.0.000679 · Cited by 40
The unraveling of substrate specificity of histone deacetylase 6 domains using acetylome peptide microarrays and peptide libraries
Kutil, Z., Skultetyova, L., Rauh, D., Meleshin, M., Šnajdr, I., Nováková, Z., Mikesova, J., Pavlı́ček, J., Hadzima, M., Baranová, P., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201801680r · Cited by 38
TgICMAP1 Is a Novel Microtubule Binding Protein in Toxoplasma gondii
Heaslip, A. T., Ems-McClung, S. C., & Hu, K. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007406 · Cited by 38
The Protein Farnesyltransferase Regulates HDAC6 Activity in a Microtubule-dependent Manner
Zhou, J., Vos, C. C., Gjyrezi, A., Yoshida, M., Khuri, F. R., Tamanoi, F., & Giannakakou, P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808708200 · Cited by 38
Self-citation
Effect of microcystin-LR on protein phosphatase 2A and its function in human amniotic epithelial cells
Liang, J. L., Tan, L., Zhang, Y., Guo, Z., & Xu, L. (2011) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b1100121 · Cited by 37
Highly acetylated tubulin permits enhanced interactions with and trafficking of plasmids along microtubules
Badding, M. A., & Dean, D. A. (2012) · Gene Therapy · doi:10.1038/gt.2012.77 · Cited by 37
Paxillin regulates cell polarization and anterograde vesicle trafficking during cell migration
Dubois, F., Alpha, K. M., & Turner, C. E. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-08-0488 · Cited by 37
CYLD – a deubiquitylase that acts to fine-tune microtubule properties and functions
Yang, Y., & Zhou, J. (2016) · Journal of Cell Science · doi:10.1242/jcs.183319 · Cited by 37
Recent development of selective inhibitors targeting the HDAC6 as anti-cancer drugs: Structure, function and design
Peng, J., Xie, F., Qin, P., Liu, Y., Niu, H., Sun, J., Xue, H., Zhao, Q., Liu, J., & Wu, J. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2023.106622 · Cited by 38
In vitro anti-cancer activity of two ethno-pharmacological healing plants from Guatemala Pluchea odorata and Phlebodium decumanum
Krupitza, G. (2009) · International Journal of Oncology · doi:10.3892/ijo_00000239 · Cited by 36
The nphp-2 and arl-13 Genetic Modules Interact to Regulate Ciliogenesis and Ciliary Microtubule Patterning in C. elegans
Warburton-Pitt, S. R. F., Silva, M., Nguyen, K. C. Q., Hall, D. H., & Barr, M. M. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004866 · Cited by 36
Mercaptoamide-based non-hydroxamic acid type histone deacetylase inhibitors
Anandan, S., Ward, J. S., Brokx, R. D., Bray, M. R., Patel, D. V., & Xiao, X.-X. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.02.075 · Cited by 36
Farnesyltransferase Inhibitors Reverse Taxane Resistance
Marcus, A. I., O’Brate, A., Buey, R. M., Zhou, J., Thomas, S. L., Khuri, F. R., Andreu, J. M., Díaz, F., & Giannakakou, P. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0699 · Cited by 36
Low molecular weight Aβ induces collapse of endoplasmic reticulum
Lai, C. S.-W., Preisler, J., Baum, L., Lee, D. H.-S., Ng, H., Hugon, J., So, K., & Chang, R. C. (2009) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2009.01.006 · Cited by 35
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
Coordination of microtubule acetylation and the actin cytoskeleton by formins
Fernández-Barrera, J., & Alonso, M. A. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2855-3 · Cited by 35
Identification of global inhibitors of cellular glycosylation
Sørensen, D. M., Büll, C., Madsen, T. D., Lira‐Navarrete, E., Clausen, T. M., Clark, A. E., Garretson, A. F., Karlsson, R. T. G., Pijnenborg, J. F. A., Yin, X., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36598-7 · Cited by 38
Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin
Arce, C. A., Casale, C. H., & Barra, H. S. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06615.x · Cited by 35
Histone Deacetylase 6 (HDAC6) Is an Independent Deacetylase for α-Tubulin
Zhao, Z., Xu, H., & Gong, W. (2010) · Protein and Peptide Letters · doi:10.2174/092986610791112620 · Cited by 35
Alcohol-induced alterations in hepatic microtubule dynamics can be explained by impaired histone deacetylase 6 function
Shepard, B. D., Joseph, R. A., Kannarkat, G. T., Rutledge, T. W., Tuma, D. J., & Tuma, P. L. (2008) · Hepatology · doi:10.1002/hep.22481 · Cited by 35
HDAC6—An Emerging Target Against Chronic Myeloid Leukemia?
Losson, H., Schnekenburger, M., Dicato, M. A., & Diederich, M. F. (2020) · Cancers · doi:10.3390/cancers12020318 · Cited by 36
HDAC6 deacetylates alpha tubulin in sperm and modulates sperm motility in Holtzman rat
Parab, S., Shetty, O. A., Gaonkar, R., Balasinor, N., Khole, V. V., & Parte, P. P. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-2039-x · Cited by 34
HDAC6 as a potential therapeutic target for peripheral nerve disorders
Prior, R. C., Helleputte, L. V., Klingl, Y. E., & Bosch, L. V. D. (2018) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2018.1541235 · Cited by 35
Autophagic degradation of KAT2A/GCN5 promotes directional migration of vascular smooth muscle cells by reducing TUBA/α-tubulin acetylation
Ouyang, C., Mu, J., Lu, Q., Li, J., Zhu, H., Wang, Q., Zou, M., & Xie, Z. (2019) · Autophagy · doi:10.1080/15548627.2019.1707488 · Cited by 32
Molecular dissection of ODF2/Cenexin revealed a short stretch of amino acids necessary for targeting to the centrosome and the primary cilium
Hüber, D., Geisler, S., Monecke, S., & Hoyer‐Fender, S. (2008) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2007.10.004 · Cited by 33
Design and Synthesis of Cyclopeptide Analogues of the Potent Histone Deacetylase Inhibitor FR235222
Gomez‐Paloma, L., Bruno, I., Cini, E., Khochbin, S., Rodriquez, M., Taddei, M., Terracciano, S., & Sadoul, K. (2007) · ChemMedChem · doi:10.1002/cmdc.200700095 · Cited by 33
Self-citation
Tubulin Acetylation and Histone Deacetylase 6 Activity in the Lung under Cyclic Load
Geiger, R., Kaufman, C. D., Lam, A. P., Budinger, G. R. S., & Dean, D. A. (2008) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2007-0307oc · Cited by 31
Honokiol ameliorates angiotensin II‐induced hypertension and endothelial dysfunction by inhibiting HDAC6‐mediated cystathionine γ‐lyase degradation
Chi, Z., Le, T. P. H., Lee, S. K., Guo, E., Kim, D., Lee, S., Seo, S., Lee, S. Y., Kim, J. H., & Lee, S. Y. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15686 · Cited by 31
Effects of trichostatin A on HIF-1α and VEGF expression in human tongue squamous cell carcinoma cells in vitro
Zuo-lin, W. (2012) · Oncology Reports · doi:10.3892/or.2012.1784 · Cited by 32
Effects of downregulated HDAC6 expression on the proliferation of lung cancer cells
Kamemura, K., Ito, A., Shimazu, T., Matsuyama, A., Maeda, S., Yao, T., Horinouchi, S., Khochbin, S., & Yoshida, M. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.06.092 · Cited by 32
Self-citation
Wild-type class I β-tubulin sensitizes Taxol-resistant breast adenocarcinoma cells harboring a β-tubulin mutation
Wiesen, K. M., Xia, S., Yang, C. H., & Horwitz, S. B. (2007) · Cancer Letters · doi:10.1016/j.canlet.2007.07.022 · Cited by 32
Synthesis and histone deacetylase inhibitory activity of cyclic tetrapeptides containing a retrohydroxamate as zinc ligand
Nishino, N., Yoshikawa, D., Watanabe, L. A., Kato, T., Jose, B., Komatsu, Y., Sumida, Y., & Yoshida, M. (2004) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2004.03.018 · Cited by 32
Self-citation
Requirement of decreased O-GlcNAc glycosylation of Mef2D for its recruitment to the myogenin promoter
Ogawa, M., Sakakibara, Y., & Kamemura, K. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.03.033 · Cited by 31
Development of a NanoBRET assay to validate inhibitors of Sirt2-mediated lysine deacetylation and defatty-acylation that block prostate cancer cell migration
Vogelmann, A., Schiedel, M., Wössner, N., Merz, A., Herp, D., Hammelmann, S., Colcerasa, A., Komaniecki, G., Hong, J., Sum, M., et al. (2022) · RSC Chemical Biology · doi:10.1039/d1cb00244a · Cited by 31
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
Whole cell microtubule analysis by flow cytometry
Morrison, K. C., & Hergenrother, P. J. (2011) · Analytical Biochemistry · doi:10.1016/j.ab.2011.08.020 · Cited by 31
Inhibition of hypoxia-induced angiogenesis by sodium butyrate, a histone deacetylase inhibitor, through hypoxia-inducible factor-1α suppression
Kim, S., Kim, K., & Jeong, J. (2007) · Oncology Reports · doi:10.3892/or.17.4.793 · Cited by 31
Acetylated tubulin associates with the fifth cytoplasmic domain of Na+/K+-ATPase: possible anchorage site of microtubules to the plasma membrane
Zampar, G. G., Chesta, M. E., Carbajal, A., Chanaday, N. L., Díaz, N. M., Casale, C. H., & Arce, C. A. (2009) · Biochemical Journal · doi:10.1042/bj20082410 · Cited by 31
Insufficient histone-3 lysine-9 deacetylation in human oocytes matured in vitro is associated with aberrant meiosis
Huang, J., Li, T., Ding, C., Brosens, J. J., Zhou, C., Wang, H. H., & Xu, Y. (2011) · Fertility and Sterility · doi:10.1016/j.fertnstert.2011.10.023 · Cited by 31
Kindlin1 regulates microtubule function to ensure normal mitosis
Patel, H., Stavrou, I., Shrestha, R. L., Draviam, V. M., Frame, M. C., & Brunton, V. G. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw009 · 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
Structure-Based Drug Designing Recommends HDAC6 Inhibitors To Attenuate Microtubule-Associated Tau-Pathogenesis
Zeb, A., Park, C., Rampogu, S. D., Son, M., Lee, G., & Lee, K. W. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00405 · Cited by 30
Phospho-HDAC6 Gathers Into Protein Aggregates in Parkinson’s Disease and Atypical Parkinsonisms
Mazzetti, S., Leonardis, M. D., Gagliardi, G., Calogero, A. M., Basellini, M. J., Madaschi, L., Costa, I., Cacciatore, F., Spinello, S., Bramerio, M., et al. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00624 · Cited by 30
In silico design of novel benzohydroxamate-based compounds as inhibitors of histone deacetylase 6 based on 3D-QSAR, molecular docking, and molecular dynamics simulations
Chu, H., He, Q., Wang, J., Hu, Y. Q., Wang, Y., & Lin, Z. (2020) · New Journal of Chemistry · doi:10.1039/d0nj04704j · Cited by 30
HDAC6 inhibition prevents TNF-α-induced caspase 3 activation in lung endothelial cell and maintains cell-cell junctions
Yu, J., Ma, M., Ma, Z., & Fu, J. (2016) · Oncotarget · doi:10.18632/oncotarget.10591 · Cited by 30
Hydroxyl Ketone-Based Histone Deacetylase Inhibitors To Gain Insight into Class I HDAC Selectivity versus That of HDAC6
Traore, M. D. M., Zwick, V., Simões‐Pires, C. A., Nurisso, A., Issa, M. E., Cuendet, M., Maynadier, M., Wein, S., Vial, H. J., Jamet, H., et al. (2017) · ACS Omega · doi:10.1021/acsomega.6b00481 · Cited by 30
Post-translational control of Myc function during differentiation
Conacci‐Sorrell, M., & Eisenman, R. N. (2011) · Cell Cycle · doi:10.4161/cc.10.4.14794 · Cited by 29
AAV9-Stathmin1 gene delivery improves disease phenotype in an intermediate mouse model of spinal muscular atrophy
Villalón, E., Kline, R., Smith, C. E., Lorson, Z. C., Osman, E. Y., O’Day, S., Murray, L. M., & Lorson, C. L. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz188 · Cited by 31
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
Role of Selective Histone Deacetylase 6 Inhibitor ACY-1215 in Cancer and Other Human Diseases
Li, J., Yu, M., Fu, S., Liu, D., & Tan, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.907981 · Cited by 29
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
Self-citation
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
Rabies Virus Infection Induces Microtubule Depolymerization to Facilitate Viral RNA Synthesis by Upregulating HDAC6
Zan, J., Liu, S., Sun, D.-N., Mo, K.-K., Yan, Y., Liu, J., Hu, B., Gu, J., Liao, M., & Zhou, J. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00146 · Cited by 29
Phosphatase inhibitor 2 promotes acetylation of tubulin in the primary cilium of human retinal epithelial cells
Wang, W., & Brautigan, D. L. (2008) · BMC Cell Biology · doi:10.1186/1471-2121-9-62 · Cited by 27
Effects of fasting on corticosterone production by zona fasciculata-reticularis cells in ovariectomized rats.
Chang, L., Kau, M., Wun, W.-S. A., Ho, L.-T., & Wang, P. S. (2002) · PubMed · Cited by 29
Protein aggregate formation in oligodendrocytes: tau and the cytoskeleton at the intersection of neuroprotection and neurodegeneration
Richter‐Landsberg, C. (2015) · Biological Chemistry · doi:10.1515/hsz-2015-0157 · Cited by 28
Deficiency of RITA results in multiple mitotic defects by affecting microtubule dynamics
Steinhäuser, K., Klöble, P., Kreis, N., Ritter, A., Friemel, A., Roth, S., Reichel, J. M., Michaelis, J., Rieger, M. A., Louwen, F., et al. (2016) · Oncogene · doi:10.1038/onc.2016.372 · Cited by 28
The viral protein gp120 decreases the acetylation of neuronal tubulin: potential mechanism of neurotoxicity
Avdoshina, V., Caragher, S. P., Wenzel, E. D., Taraballi, F., Mocchetti, I., & Harry, G. J. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14015 · Cited by 28
The paxillin-plectin-EPLIN complex promotes apical elimination of RasV12-transformed cells by modulating HDAC6-regulated tubulin acetylation
Kasai, N., Kadeer, A., Kajita, M., Saitoh, S., Ishikawa, S., Maruyama, T., & Fujita, Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-20146-1 · Cited by 28
Targeting histone deacetylase in thyroid cancer
Russo, D., Durante, C., Bulotta, S., Puppin, C., Puxeddu, E., Filetti, S., & Damante, G. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.740013 · Cited by 28

Authors: Matsuyama, A., Shimazu, T., Sumida, Y., Saito, A., Yoshimatsu, Y., Seigneurin‐Berny, D., Osada, H., Komatsu, Y., Nishino, N., Khochbin, S., Horinouchi, S., & Yoshida, M.
Affiliations: RIKEN (JP)
The University of Tokyo (JP)
Inserm (FR)
Kyushu Institute of Technology (JP)
Corresponding author: Yoshida, Minoru
ORCID: Matsuyama, Akihisa
Yoshimatsu, Yasuhiro
Seigneurin‐Berny, Daphné
Khochbin, Saadi
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2002-12-16
Volume: 21
Issue: 24
Pages: 6820-6831
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1093/emboj/cdf682
PMC: PMC139102
OpenAlex: W2148495272
Cited by: 720
References: 45
Citations by year: 2026: 18 · 2025: 16 · 2024: 14 · 2023: 27 · 2022: 15 · 2021: 28 · 2020: 25 · 2019: 29 · 2018: 27 · 2017: 33 · 2016: 35 · 2015: 36 · 2014: 34 · 2013: 45 · 2012: 45
FWCI: 7.65
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: Japan Science and Technology Corporation (CREST)
Core Research for Evolutional Science and Technology
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, histone deacetylase, alpha-tubulin, tubulin acetylation, microtubule stability, microtubule dynamics, microtubule depolymerization, trichostatin A, class II HDACs, tubulin deacetylation, microtubule turnover
MeSH terms: Histone Deacetylase 6, Acetylation, Ethanol, Animals, Antineoplastic Agents, Phytogenic, Demecolcine, Histone Deacetylases, Microscopy, Fluorescence, Microtubules, Peptides, Plasmids, Precipitin Tests, Protein Binding, Time Factors, Transfection, Tubulin, Immunoblotting, NIH 3T3 Cells, Mice

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

In vivo destabilization of dynamic microtubules by HDAC6‐mediated deacetylation

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks