Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
Open accessAbstract
Protein acetylation, especially histone acetylation, is the subject of both research and clinical investigation. At least four small-molecule histone deacetylase inhibitors are currently in clinical trials for the treatment of cancer. These and other inhibitors also affect microtubule acetylation. A multidimensional, chemical genetic screen of 7,392 small molecules was used to discover “tubacin,” which inhibits α-tubulin deacetylation in mammalian cells. Tubacin does not affect the level of histone acetylation, gene-expression patterns, or cell-cycle progression. We provide evidence that class II histone deacetylase 6 (HDAC6) is the intracellular target of tubacin. Only one of the two catalytic domains of HDAC6 possesses tubulin deacetylase activity, and only this domain is bound by tubacin. Tubacin treatment did not affect the stability of microtubules but did decrease cell motility. HDAC6 overexpression disrupted the localization of p58, a protein that mediates binding of Golgi elements to microtubules. Our results highlight the role of α-tubulin acetylation in mediating the localization of microtubule-associated proteins. They also suggest that small molecules that selectively inhibit HDAC6-mediated α-tubulin deacetylation, a first example of which is tubacin, might have therapeutic applications as antimetastatic and antiangiogenic agents.
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Treatment of cells with a tubulin deacetylase HDAC6 inhibitor (tubacin) or overexpression of the tubulin acetylase αTAT1 did not inhibit the binding of GEF-H1 to microtubules.
“Moreover, treatment of cells with a tubulin deacetylase HDAC6 inhibitor (tubacin 54 ) or overexpression of the tubulin acetylase αTAT1 55 , both of which caused acetylation of all cellular microtubules, did not inhibit the binding of GEF-H1 to microtubules (Fig. 3a,d and Extended Data Fig. 4a,d).”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [54]
Inhibition of tubulin deacetylase HDAC6 using tubacin produced a significant accumulation of acetylated microtubules.
“We observed that inhibition of tubulin deacetylase HDAC6 using tubacin produced a significant accumulation of acetylated microtubules [44]”
HDAC6 is the deacetylase for a diverse set of substrates involved in tumourigenesis, such as HSP90, α-tubulin, cortactin and peroxiredoxins.
“HDAC6 was shown to be the deacetylase for a diverse set of substrates involved in tumourigenesis, such as HSP90, α-tubulin, cortactin and peroxiredoxins”
From A novel small molecule hydroxamate preferentially inhibits HDAC6 activity and tumour growth (2013) · cites this paper as Haggarty et al, 2003
HDAC6 selective inhibitors (tubacin, tubastatin A) have only contributed to validate HDAC6 as a target.
“To date, HDAC6 selective inhibitors (tubacin, tubastatin A) have only contributed to validate HDAC6 as a target”
From A novel small molecule hydroxamate preferentially inhibits HDAC6 activity and tumour growth (2013) · cites this paper as Haggarty et al, 2003
HDAC6 selective inhibitors (tubacin, tubastatin A) have unfavourable pharmacokinetic profiles that have prevented them from further pre-clinical and clinical development.
“their unfavourable pharmacokinetic (PK) profiles have prevented them from further pre-clinical and clinical development, making them only good research tools”
From A novel small molecule hydroxamate preferentially inhibits HDAC6 activity and tumour growth (2013) · cites this paper as Haggarty et al, 2003
Inhibition of HDAC6 is believed not to be associated with severe toxicity.
“unlike other HDACs, inhibition of HDAC6 is believed not to be associated with severe toxicity”
From A novel small molecule hydroxamate preferentially inhibits HDAC6 activity and tumour growth (2013) · cites this paper as Haggarty et al, 2003
HDAC6 knockout in mice does not lead to embryonic lethality.
“HDAC6 knockout in mice does not lead to embryonic lethality”
From A novel small molecule hydroxamate preferentially inhibits HDAC6 activity and tumour growth (2013) · cites this paper as Haggarty et al, 2003
Tubacin's non-drug-like structure, high lipophilicity, and tedious synthesis make it more useful as a research tool than a drug.
“The use of Tubacin in models of disease has helped to validate, in part, HDAC6 as a drug target, but its non-drug-like structure, high lipophilicity (ClogP = 6.36 (KOWWIN)), and tedious synthesis conspire to make it more useful as a research tool than a drug.21”
From Rational Design and Simple Chemistry Yield a Superior, Neuroprotective HDAC6 Inhibitor, Tubastatin A (2010) · cites this paper as [21]
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Cites
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403 · see citing works
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 · see citing works
A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829 · see citing works
Self-citationPhiel, C. J., Zhang, F., Huang, E. Y., Guenther, M. G., Lazar, M. A., & Klein, P. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101287200 · Cited by 1,758 · see citing works
Small Molecule Inhibitor of Mitotic Spindle Bipolarity Identified in a Phenotype-Based Screen
Mayer, T. U., Kapoor, T. M., Haggarty, S. J., King, R. W., Schreiber, S. L., & Mitchison, T. J. (1999) · Science · doi:10.1126/science.286.5441.971 · Cited by 1,732 · see citing works
Self-citationHistone-deacetylase inhibitors: novel drugs for the treatment of cancer
Johnstone, R. W. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd772 · Cited by 1,515 · see citing works
Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
Steffan, J. S., Bodai, L., Pallos, J., Poelman, M., McCampbell, A., Apostol, B. L., Kazantsev, A., Schmidt, E., Zhu, Y.-Z., Greenwald, M., et al. (2001) · Nature · doi:10.1038/35099568 · Cited by 1,228 · see citing works
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 · see citing works
Three proteins define a class of human histone deacetylases related to yeast Hda1p
Grozinger, C. M., Hassig, C. A., & Schreiber, S. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4868 · Cited by 770 · see citing works
Self-citationIn vivo destabilization of dynamic microtubules by HDAC6‐mediated deacetylation
Matsuyama, A., Shimazu, T., Sumida, Y., Saito, A., Yoshimatsu, Y., Seigneurin‐Berny, D., Osada, H., Komatsu, Y., Nishino, N., Khochbin, S., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf682 · Cited by 720 · see citing works
Grozinger, C. M., & Schreiber, S. L. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00092-3 · Cited by 537 · see citing works
Self-citationKijima, M., Yoshida, M., Sugita, K., Horinouchi, S., & Beppu, T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41547-5 · Cited by 516 · see citing works
Furumai, R., Komatsu, Y., Nishino, N., Khochbin, S., Yoshida, M., & Horinouchi, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.1.87 · Cited by 412 · see citing works
Signaling Network Model of Chromatin
Schreiber, S. L., & Bernstein, B. (2002) · Cell · doi:10.1016/s0092-8674(02)01196-0 · Cited by 395 · see citing works
Self-citationFunctional significance of histone deacetylase diversity
Khochbin, S., Verdel, A., Lemercier, C., & Seigneurin-Berny, D. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00174-x · Cited by 366 · see citing works
A role for histone deacetylase activity in HDAC1-mediated transcriptional repression
Hassig, C. A., Tong, J. K., Fleischer, T. C., Owa, T., Grable, P. G., Ayer, D. E., & Schreiber, S. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3519 · Cited by 365 · see citing works
Self-citationTaddei, A., Maison, C., Roche, D., & Almouzni, G. (2001) · Nature Cell Biology · doi:10.1038/35055010 · Cited by 361 · see citing works
Polyploid formation in cotton is not accompanied by rapid genomic changes
Liu, B., Brubaker, C. L., Mergeai, G., et al. (2001) · Genome · doi:10.1139/g01-011 · Cited by 356 · see citing works
Role of Microtubules in the Organization of the Golgi Complex
Thyberg, J., & Moskalewski, S. (1999) · Experimental Cell Research · doi:10.1006/excr.1998.4326 · Cited by 342 · see citing works
Schadt, E. E., Cheng, L., Ellis, B., & Wong, W. H. (2001) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10073 · Cited by 288 · see citing works
Tubulin acetylation and cell motility
Palazzo, A., Ackerman, B., & Gundersen, G. G. (2003) · Nature · doi:10.1038/421230a · Cited by 256 · see citing works
The diversity of acetylated proteins.
Polevoda, B. V., & Sherman, F. (2002) · Genome biology · doi:10.1186/gb-2002-3-5-reviews0006 · Cited by 253 · see citing works
Stockwell, B. R., Haggarty, S. J., & Schreiber, S. L. (1999) · Chemistry & Biology · doi:10.1016/s1074-5521(99)80004-0 · Cited by 203 · see citing works
Self-citationHaggarty, S. J., Koeller, K. M., Wong, J. C., Butcher, R. A., & Schreiber, S. L. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00095-4 · Cited by 201 · see citing works
Self-citationHempen, B., & Brion, J. (1996) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199609000-00003 · Cited by 177 · see citing works
Sternson, S. M., Wong, J. C., Grozinger, C. M., & Schreiber, S. L. (2001) · Organic Letters · doi:10.1021/ol016915f · Cited by 139 · see citing works
Self-citationA one-bead, one-stock solution approach to chemical genetics: part 1
Blackwell, H. E., Pérez, L., Stavenger, R. A., Tallarico, J. A., Cope-Eatough, E. K., Foley, M. A., & Schreiber, S. L. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(01)00085-0 · Cited by 125 · see citing works
Self-citationA one-bead, one-stock solution approach to chemical genetics: part 2
Clemons, P. A., Koehler, A. N., Wagner, B. K., Sprigings, T. G., Spring, D. R., King, R. W., Schreiber, S. L., & Foley, M. A. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(01)00086-2 · Cited by 107 · see citing works
Self-citationDynamics of alpha-tubulin deacetylation in intact neurons
Black, M., Baas, P. W., & Humphries, S. V. (1989) · Journal of Neuroscience · doi:10.1523/jneurosci.09-01-00358.1989 · Cited by 92 · see citing works
Chemical Genetic Modifier Screens
Koeller, K. M., Haggarty, S. J., Perkins, B. D., Leykin, I., Wong, J. C., Kao, M.-C. J., & Schreiber, S. L. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00093-0 · Cited by 89 · see citing works
Self-citationSaragoni, L., Hernández, P., & Maccioni, R. B. (2000) · Neurochemical Research · doi:10.1023/a:1007587315630 · Cited by 42 · see citing works
Involvement of glycogen synthase kinase‐3β and tau phosphorylation in neuronal Golgi disassembly
Elyaman, W., Yardin, C., & Hugon, J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00838.x · Cited by 34 · see citing works
Recent advances in the discovery of small molecule histone deacetylase inhibitors.
Remiszewski, S. (2002) · PubMed · Cited by 34 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
A Next Generation Connectivity Map: L1000 Platform and the First 1,000,000 Profiles
Subramanian, A., Narayan, R., Corsello, S. M., Peck, D. D., Natoli, T. E., Lu, X., Gould, J., Davis, J. F., Tubelli, A. A., Asiedu, J. K., et al. (2017) · Cell · doi:10.1016/j.cell.2017.10.049 · Cited by 3,515 · see citing works
Self-citationHistone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders
Falkenberg, K. J., & Johnstone, R. W. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4360 · Cited by 1,564 · see citing works
New and emerging HDAC inhibitors for cancer treatment
West, A. C., & Johnstone, R. W. (2014) · Journal of Clinical Investigation · doi:10.1172/jci69738 · Cited by 1,404 · see citing works
HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153 · see citing works
Targeting epigenetic regulators for cancer therapy: mechanisms and advances in clinical trials
Cheng, Y., He, C., Wang, M., Ma, X., Mo, F., Yang, S., Han, J., & Wei, X. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0095-0 · Cited by 1,097 · see citing works
HDAC family: What are the cancer relevant targets?
Witt, O., Deubzer, H. E., Milde, T., & Oehme, I. (2009) · Cancer Letters · doi:10.1016/j.canlet.2008.08.016 · Cited by 1,069 · see citing works
Rational Design and Simple Chemistry Yield a Superior, Neuroprotective HDAC6 Inhibitor, Tubastatin A
Butler, K. V., Kalin, J., Brochier, C., Vistoli, G., Langley, B., & Kozikowski, A. P. (2010) · Journal of the American Chemical Society · doi:10.1021/ja102758v · Cited by 801 · see citing works
Dompierre, J. P., Godin, J. D., Charrin, B. C., Cordelières, F. P., King, S. J., Humbert, S., & Saudou, F. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.0037-07.2007 · Cited by 792 · see citing works
Bali, P., Pranpat, M., Bradner, J., Balasis, M., Fiskus, W., Guo, F., Rocha, K., Kumaraswamy, S., Boyapalle, S., Atadja, P., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500186200 · Cited by 755 · see citing works
HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin.
Iwata, A., Riley, B. E., Johnston, J. A., & Kopito, R. R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508786200 · Cited by 719 · see citing works
Multiple roles of HDAC inhibition in neurodegenerative conditions
Chuang, D.-M., Leng, Y., Marinova, Z., Kim, H.-J., & Chiu, C.-T. (2009) · Trends in Neurosciences · doi:10.1016/j.tins.2009.06.002 · Cited by 676 · see citing works
HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics
Gallinari, P., Marco, S. D., Jones, P., Pallaoro, M., & Steinkühler, C. (2007) · Cell Research · doi:10.1038/sj.cr.7310149 · Cited by 678 · see citing works
Diversity-oriented synthesis: Exploring the intersections between chemistry and biology
Tan, D. S. (2005) · Nature Chemical Biology · doi:10.1038/nchembio0705-74 · Cited by 605 · see citing works
Histone deacetylase 6 structure and molecular basis of catalysis and inhibition
Hai, Y., & Christianson, D. W. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2134 · Cited by 521 · see citing works
“Initial studies indicated that both domains are catalytically active toward histone substrates, with only CD2 exhibiting tubulin deacetylase activity, 19,29 whereas subsequent studies suggested that only CD2 is catalytically active.”
Protein Homeostasis and Aging: the importance of exquisite quality control
Koga, H., Kaushik, S., & Cuervo, A. M. (2011) · Ageing research reviews · doi:10.1016/j.arr.2010.02.001 · Cited by 476 · see citing works
Balasubramanian, S., Ramos, J., Luo, W., Sirisawad, M., Verner, E., & Buggy, J. J. (2008) · Leukemia · doi:10.1038/leu.2008.9 · Cited by 458 · see citing works
Targeted Cancer Therapy: Giving Histone Deacetylase Inhibitors All They Need To Succeed
Gryder, B. E., Sodji, Q. H., & Oyelere, A. K. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.3 · Cited by 404 · see citing works
Histone deacetylase 8 in neuroblastoma tumorigenesis
Oehme, I., Deubzer, H. E., Wegener, D., Pickert, D., Linke, J.-P., Hero, B., Kopp-Schneider, A., Westermann, F., Ulrich, S. M., von Deimling, A., et al. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-0684 · Cited by 398 · see citing works
HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination
Boyault, C., Sadoul, K., Pabion, M., & Khochbin, S. (2007) · Oncogene · doi:10.1038/sj.onc.1210614 · Cited by 397 · see citing works
Chemical substructures that enrich for biological activity
Klekota, J., & Roth, F. P. (2008) · Bioinformatics · doi:10.1093/bioinformatics/btn479 · Cited by 392 · see citing works
Histone deacetylase 6 interacts with the microtubule‐associated protein tau
Ding, H., Dolan, P. J., & Johnson, G. V. W. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05564.x · Cited by 387 · see citing works
The epigenetics of aging and neurodegeneration
Lardenoije, R., Iatrou, A., Kenis, G., Kompotis, K., Steinbusch, H. W. M., Mastroeni, D., Coleman, P., Lemere, C. A., Hof, P. R., van den Hove, D. L. A., et al. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.002 · Cited by 381 · see citing works
Isoform-selective histone deacetylase inhibitors
Bieliauskas, A. V., & Pflum, M. K. H. (2008) · Chemical Society Reviews · doi:10.1039/b703830p · Cited by 350 · see citing works
Shukla, S., & Tekwani, B. L. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00537 · Cited by 314 · see citing works
Small molecules: the missing link in the central dogma
Schreiber, S. L. (2005) · Nature Chemical Biology · doi:10.1038/nchembio0705-64 · Cited by 306 · see citing works
Self-citationThe Cytoplasmic Deacetylase HDAC6 Is Required for Efficient Oncogenic Tumorigenesis
Lee, Y.-S., Lim, K.-H., Guo, X., Kawaguchi, Y., Gao, Y., Barrientos, T., Ordentlich, P., Wang, X.-F., Counter, C. M., & Yao, T.-P. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0188 · Cited by 260 · see citing works
Primary Cilia and the Cell Cycle
Plotnikova, O. V., Pugacheva, E. N., & Golemis, E. A. (2009) · Methods in Cell Biology · doi:10.1016/s0091-679x(08)94007-3 · Cited by 236 · see citing works
Therapeutic potential for HDAC inhibitors in the heart
McKinsey, T. A. (2012) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134712 · Cited by 230 · see citing works
Histone deacetylase 10 promotes autophagy-mediated cell survival
Oehme, I., Linke, J.-P., Böck, B. C., Milde, T., Lodrini, M., Hartenstein, B., Wiegand, I., Eckert, C., Roth, W., Kool, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300113110 · Cited by 221 · see citing works
Lineage specificity of primary cilia in the mouse embryo
Bangs, F. K., Schrode, N., Hadjantonakis, A.-K., & Anderson, K. V. (2015) · Nature Cell Biology · doi:10.1038/ncb3091 · Cited by 174 · see citing works
Halili, M. A., Andrews, M. R., Labzin, L. I., Schroder, K., Matthias, G., Cao, C., Lovelace, E., Reid, R. C., Le, G. T., Hume, D. A., et al. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.0509363 · Cited by 186 · see citing works
Recent advances in the discovery of potent and selective HDAC6 inhibitors
Wang, X.-X., Wan, R.-Z., & Liu, Z.-P. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.10.040 · Cited by 152 · see citing works
Development of a histone deacetylase 6 inhibitor and its biological effects
Lee, J.-H., Mahendran, A., Yao, Y., Ngo, L., Venta-Perez, G., Choy, M. L., Kim, N., Ham, W.-S., Breslow, R., & Marks, P. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313893110 · Cited by 141 · see citing works
Strategies To Design Selective Histone Deacetylase Inhibitors
Melesina, J., Simoben, C. V., Praetorius, L., Bülbül, E. F., Robaa, D., & Sippl, W. (2021) · ChemMedChem · doi:10.1002/cmdc.202000934 · Cited by 118 · see citing works
Porter, N. J., Osko, J. D., Diedrich, D., Kurz, T., Hooker, J. M., Hansen, F. K., & Christianson, D. W. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01013 · Cited by 111 · see citing works
Vögerl, K., Ong, N., Senger, J., Herp, D., Schmidtkunz, K., Marek, M., Müller, M., Bartel, K., Shaik, T. B., Porter, N. J., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01090 · Cited by 104 · see citing works
Chemical Genetic Modifier Screens
Koeller, K. M., Haggarty, S. J., Perkins, B. D., Leykin, I., Wong, J. C., Kao, M.-C. J., & Schreiber, S. L. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00093-0 · Cited by 89 · see citing works
Self-citationA novel small molecule hydroxamate preferentially inhibits HDAC6 activity and tumour growth
Kaliszczak, M., Trousil, S., Åberg, O., Perumal, M., Nguyen, Q.-D., & Aboagye, E. O. (2013) · British Journal of Cancer · doi:10.1038/bjc.2012.576 · Cited by 66 · see citing works
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 · see citing works
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 · see citing works
Nielsen, B. S., Malinda, R. R., Schmid, F. M., Pedersen, S. F., Christensen, S. T., & Pedersen, L. B. (2015) · Journal of Cell Science · doi:10.1242/jcs.173559 · Cited by 36 · see citing works
OptoTAT reveals microtubule acetylation as a rapid trigger for GEF-H1–mediated cell migration
Deb Roy, A., Gonzalez, C. S., Stanislauskas, M., Shahid, F., Yadav, E., Rezek, J., & Inoue, T. (2026) · Journal of Cell Biology · doi:10.1083/jcb.202508095 · Cited by 2 · see citing works
Meiring, J. C. M., Mahapatra, V., Liu, R., Gravett, M. S. C., Morren, D., Saunders, H. A. J., Choi, S. R., Pelster José, A., Karhanova, A., Metallidou, I., et al. (2026) · Nature Cell Biology · doi:10.1038/s41556-026-02079-4
Asensio‐Juárez, G., Pérez‐Díaz, R., Ramos‐Solano, H., Garrido‐Casado, M., Talayero, V. C., & Vicente‐Manzanares, M. (2026) · Molecular Oncology · doi:10.1002/1878-0261.70333
- Authors
- Haggarty, S. J., Koeller, K. M., Wong, J. C., Grozinger, C. M., & Schreiber, S. L.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2003-04-03
- Volume
- 100
- Issue
- 8
- Pages
- 4389-4394
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC153564
- OpenAlex
- W2101127235
- Cited by
- 1,066
- References
- 33
- Citations by year
- 2026: 29 · 2025: 22 · 2024: 30 · 2023: 33 · 2022: 29 · 2021: 32 · 2020: 50 · 2019: 39 · 2018: 55 · 2017: 54 · 2016: 47 · 2015: 70 · 2014: 53 · 2013: 59 · 2012: 58
- FWCI
- 13.10
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- 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
- Physical Sciences › Chemistry › Organic Chemistry › Synthesis and biological activity
- Keywords
- tubacin, HDAC6, alpha-tubulin deacetylation, microtubule acetylation, small molecule inhibitors, chemical genetic screen, p58, cell motility, anti-metastatic agents, angiogenesis inhibitors, histone deacetylase inhibitors
- MeSH terms
- Histone Deacetylase 6, Acetylation, Anilides, Animals, Cell Cycle, Cell Line, Dioxanes, Drug Evaluation, Preclinical, Enzyme Inhibitors, Histone Deacetylases, Humans, Hydroxamic Acids, Microtubule-Associated Proteins, Microtubules, Recombinant Proteins, Tubulin, Gene Expression, 3T3 Cells, Protein Structure, Tertiary, Jurkat Cells, Mice, Histone Deacetylase Inhibitors
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 ›
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