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 accessAbstract
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.
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“HDAC6, a tubulin deacetylase [24].”
From Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons (2026) · cites this paper as [31]
In the citing paper
“Acelylation of α-tubulin, which promotes microtubule stabilisation, may distort mitosis and trigger apoptosis (Matsuyama et al, 2002); it can also affect changes in cell motility and, hence, invasion and metastasis of cancer cells (Hubbert et al, 2002).”
From A novel small molecule hydroxamate preferentially inhibits HDAC6 activity and tumour growth (2013) · cites this paper as Matsuyama et al, 2002
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Cites
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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
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Self-citationAcetylation 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.
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Haberland, M., Montgomery, R. L., & Olson, E. N. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2485 · Cited by 2,600
Acetylation and deacetylation of non-histone proteins
Glozak, M. A., Sengupta, N., Zhang, X., & Seto, E. (2005) · Gene · doi:10.1016/j.gene.2005.09.010 · Cited by 1,584
Kawaguchi, Y., Kovacs, J. J., McLaurin, A. C., Vance, J. M., Ito, A., & Yao, T. (2003) · Cell · doi:10.1016/s0092-8674(03)00939-5 · Cited by 1,529
Gregoretti, I., Lee, Y.-M., & Goodson, H. V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.006 · Cited by 1,456
The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men
Yang, X., & Seto, E. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2346 · Cited by 1,277
Metadata
- 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
- Venue
- The EMBO Journal
- Published
- 2002-12-16
- Volume
- 21
- Issue
- 24
- Pages
- 6820-6831
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- 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
- 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
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