The tubulin code and its role in controlling microtubule properties and functions
Open accessAbstract
Microtubules are core components of the eukaryotic cytoskeleton with essential roles in cell division, shaping, motility and intracellular transport. Despite their functional heterogeneity, microtubules have a highly conserved structure made from almost identical molecular building blocks: the tubulin proteins. Alternative tubulin isotypes and a variety of post-translational modifications control the properties and functions of the microtubule cytoskeleton, a concept known as the 'tubulin code'. Here we review the current understanding of the molecular components of the tubulin code and how they impact microtubule properties and functions. We discuss how tubulin isotypes and post-translational modifications control microtubule behaviour at the molecular level and how this translates into physiological functions at the cellular and organism levels. We then go on to show how fine-tuning of microtubule function by some tubulin modifications can affect homeostasis and how perturbation of this fine-tuning can lead to a range of dysfunctions, many of which are linked to human disease.
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Disruption of microtubule-facilitated movement and segregation of chromosomes during mitosis induces mitotic arrest and apoptosis in rapidly dividing cancer cells.
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Lattice conformation is emerging as an important, understudied constituent of the 'tubulin code'.
“Next to microtubule post-translational modifications and tubulin isotypes, lattice conformation is emerging as an important, understudied constituent of the 'tubulin code', the structural, biochemical and functional diversification of microtubule subsets in the same cell 68-70 .”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [68]
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
Genes and molecular pathways underpinning ciliopathies
Reiter, J. F., & Leroux, M. R. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.60 · Cited by 1,588 · see citing works
HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS.
Pandey, U. B., Nie, Z., Batlevi, Y., McCray, B. A., Ritson, G. P., Nedelsky, N. B., Schwartz, S. L., DiProspero, N. A., Knight, M. A., Schuldiner, O., et al. (2007) · Nature · doi:10.1038/nature05853 · Cited by 1,234 · see citing works
HDAC6 controls autophagosome maturation essential for ubiquitin‐selective quality‐control autophagy
Lee, J., Koga, H., Kawaguchi, Y., Tang, W., Wong, E., Gao, Y., Pandey, U. B., Kaushik, S., Tresse, E., Lu, J., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.405 · Cited by 756 · see citing works
Mice Lacking Histone Deacetylase 6 Have Hyperacetylated Tubulin but Are Viable and Develop Normally
Zhang, Y., Kwon, S., Yamaguchi, T., Cubizolles, F., Rousseaux, S., Kneissel, M., Cao, C., Li, N., Cheng, H.-L., Chua, K., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01154-06 · Cited by 559 · see citing works
HDAC6 inhibition reverses axonal transport defects in motor neurons derived from FUS-ALS patients
Guo, W., Naujock, M., Fumagalli, L., Vandoorne, T., Baatsen, P., Boon, R., Ordovás, L., Patel, A., Welters, M., Vanwelden, T., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00911-y · Cited by 373 · see citing works
Axonal transport: Driving synaptic function
Guedes-Dias, P., & Holzbaur, E. L. F. (2019) · Science · doi:10.1126/science.aaw9997 · Cited by 355 · see citing works
Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation
Aillaud, C., Bosc, C., Peris, L., Bosson, A., Heemeryck, P., Van Dijk, J., Le Friec, J., Boulan, B., Vossier, F., Sanman, L. E., et al. (2017) · Science · doi:10.1126/science.aao4165 · Cited by 293 · see citing works
The Deacetylase HDAC6 Mediates Endogenous Neuritic Tau Pathology
Tseng, J.-H., Xie, L., Song, S., Xie, Y., Allen, L., Ajit, D., Hong, J.-S., Chen, X., Meeker, R. B., & Cohen, T. J. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.082 · Cited by 93 · see citing works
Detyrosinated microtubules spatially constrain lysosomes facilitating lysosome-autophagosome fusion
Mohan, N., Sorokina, E. M., Verdeny, I. V., Alvarez, A. S., & Lakadamyali, M. (2019) · Journal of Cell Biology · doi:10.1083/jcb.201807124 · Cited by 92 · see citing works
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Wang, Z., Li, H., Gou, L., Li, W., & Wang, Y. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.06.015 · Cited by 264 · see citing works
Posttranslational modification of microtubules by the MATCAP detyrosinase
Landskron, L., Bak, J., Adamopoulos, A., Kaplani, K., Moraiti, M., van den Hengel, L. G., Song, J.-Y., Bleijerveld, O. B., Nieuwenhuis, J., Heidebrecht, T., et al. (2022) · Science · doi:10.1126/science.abn6020 · Cited by 78 · see citing works
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Wu, D., Li, Y., Zheng, L., Xiao, H., Ouyang, L., Wang, G., & Sun, Q. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.05.035 · Cited by 71 · see citing works
A live-cell marker to visualize the dynamics of stable microtubules throughout the cell cycle
Jansen, K. I., Iwanski, M. K., Burute, M., & Kapitein, L. C. (2023) · Journal of Cell Biology · doi:10.1083/jcb.202106105 · Cited by 39 · see citing works
StableMARK-decorated microtubules in cells have expanded lattices
de Jager, L., Jansen, K. I., Hoogebeen, R., Akhmanova, A., Kapitein, L. C., Förster, F., & Howes, S. C. (2025) · Journal of Cell Biology · doi:10.1083/jcb.202206143 · Cited by 25 · see citing works
The evolving landscape of antibody-drug conjugates (ADCs) for treatment of prostate cancer
Lin, C., Hadfield, M. J., Santopietro, A., Lagos, G., Cheng, L., El-Deiry, W. S., Aggarwal, R., Mega, A., Hyams, E., & Carneiro, B. A. (2025) · npj Precision Oncology · doi:10.1038/s41698-025-01131-0 · Cited by 20 · 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
- Authors
- Janke, C., & Magiera, M. M.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Janke, Carsten
- Magiera, Maria M.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2020-02-27
- Volume
- 21
- Issue
- 6
- Pages
- 307-326
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W3007078842
- Cited by
- 956
- References
- 10
- Citations by year
- 2026: 142 · 2025: 189 · 2024: 172 · 2023: 146 · 2022: 152 · 2021: 114 · 2020: 41
- FWCI
- 13.28
- Type
- journal article
- Language
- en
- Open access
- green
- hal.science
- Licence
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Funders
- Agence Nationale de la Recherche (ANR-17-CE13-0021, ANR-10-IDEX-0001, ANR-12-BSV2-0007)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- tubulin code, microtubules, tubulin isoforms, post-translational modification, microtubule dynamics, microtubule-associated proteins, cytoskeleton, cell division, intracellular transport, neurodegenerative diseases
- MeSH terms
- Animals, Cell Division, Cell Movement, Cytoskeleton, Humans, Microtubule-Associated Proteins, Microtubules, Protein Processing, Post-Translational, Tubulin, Protein Isoforms
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