Tubulin Posttranslational Modifications and Emerging Links to Human Disease

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

Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation

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

Purkinje cell degeneration, a new neurological mutation in the mouse.

Mullen, R. J., Eicher, E. M., & Sidman, R. L. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.1.208 · Cited by 611

The tubulin code: Molecular components, readout mechanisms, and functions

Janke, C. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201406055 · Cited by 534

Microtubules acquire resistance from mechanical breakage through intralumenal acetylation

Xu, Z., Schaedel, L., Portran, D., Aguilar, A., Gaillard, J., Marinkovich, M. P., Théry, M., & Nachury, M. V. (2017) · Science · doi:10.1126/science.aai8764 · Cited by 505

HDAC6 inhibitors reverse axonal loss in a mouse model of mutant HSPB1–induced Charcot-Marie-Tooth disease

d’Ydewalle, C. V. O., Krishnan, J., Chiheb, D., Damme, P. V., Irobi, J., Kozikowski, A. P., Berghe, P. V., Timmerman, V., Robberecht, W., & Bosch, L. V. D. (2011) · Nature Medicine · doi:10.1038/nm.2396 · Cited by 462

A Family of Protein-Deglutamylating Enzymes Associated with Neurodegeneration

Rogowski, K., van Dijk, J., Magiera, M. M., Bosc, C., Deloulme, J., Bosson, A., Peris, L., Gold, N. D., Lacroix, B., Bosch, M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.10.014 · Cited by 397

Centriole Disassembly In Vivo and Its Effect on Centrosome Structure and Function in Vertebrate Cells

Bobinnec, Y., Khodjakov, A. L., Mir, L. M., Rieder, C. L., Eddé, B., & Bornens, M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.6.1575 · Cited by 378

Post-translational modifications of tubulin: pathways to functional diversity of microtubules

Song, Y., & Brady, S. T. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.10.004 · Cited by 377

Detyrosinated microtubules buckle and bear load in contracting cardiomyocytes

Robison, P., Caporizzo, M. A., Ahmadzadeh, H., Bogush, A. I., Chen, C. Y., Margulies, K. B., Shenoy, V. B., & Prosser, B. L. (2016) · Science · doi:10.1126/science.aaf0659 · Cited by 338

(De)glutamylation and cell death in Leishmania parasites

Basmaciyan, L., Robinson, D. R., Azas, N., & Casanova, M. (2019) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0007264 · Cited by 9

α-Tubulin acetylation at lysine 40 regulates dendritic arborization and larval locomotion by promoting microtubule stability in Drosophila

Niu, X., Mao, C., Wang, S., Wang, X., Zhang, Y., Hu, J., Bi, R., Liu, Z., & Jin, S. (2023) · PLoS ONE · doi:10.1371/journal.pone.0280573 · Cited by 8

Tubulin Carboxypeptidase Activity Promotes Focal Gelatin Degradation in Breast Tumor Cells and Induces Apoptosis in Breast Epithelial Cells That Is Overcome by Oncogenic Signaling

Mathias, T. J., Ju, J. A., Lee, R., Thompson, K. N., Mull, M. L., Annis, D. A., Chang, K. T., Ory, E. C., Stemberger, M. B., Hotta, T., et al. (2022) · Cancers · doi:10.3390/cancers14071707 · Cited by 8

Altering microtubule stability affects microtubule clearance and nuclear extrusion during erythropoiesis

Xie, S., Yan, B., Feng, J., Wu, Y., He, N., Sun, L., Zhou, J., Li, D., & Liu, M. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28582 · Cited by 6

Alteration of Neural Stem Cell Functions in Ataxia and Male Sterility Mice: A Possible Role of β-Tubulin Glutamylation in Neurodegeneration

Sheikh, A. M., Yano, S., Tabassum, S., Omura, K., Araki, A., Mitaki, S., Ito, Y., Huang, S., & Nagai, A. (2021) · Cells · doi:10.3390/cells10010155 · Cited by 7

Inhibition of acetyl-CoA carboxylase impaired tubulin palmitoylation and induced spindle abnormalities

Fang, C.-T., Kuo, H., Amartuvshin, O., Hsu, H., Liu, S.-L., Yao, J.-S., & Yih, L. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01301-8 · Cited by 8

Effects of P301L-TAU on post-translational modifications of microtubules in human iPSC-derived cortical neurons and TAU transgenic mice

Kabbani, M. A. A., Köhler, C. N., & Zempel, H. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01742 · Cited by 6

Mechanistic insights into TTLL11 polyglutamylase–mediated primary tubulin chain elongation

Campbell, J., Vošahlíková, M., Ismail, S., Volnikova, M., Motlova, L., Kudlacova, J., Ustinova, K., Šnajdr, I., Nováková, Z., Basta, M., et al. (2025) · Science Advances · doi:10.1126/sciadv.adw1561 · Cited by 6

More is not always better: hyperglutamylation leads to neurodegeneration

Akhmanova, A. S., & Hoogenraad, C. C. (2018) · The EMBO Journal · doi:10.15252/embj.2018101023 · Cited by 6

Actin: Post-translational Modification of Actin Linked to Formin Inhibition

Domínguez, R. (2019) · Current Biology · doi:10.1016/j.cub.2019.03.061 · Cited by 6

Effect of TTLL12 on tubulin tyrosine nitration as a novel target for screening anticancer drugs in vitro

Xue, L., Zeng, Y., Fang, C., Cheng, W. N., & Li, Y. (2020) · Oncology Letters · doi:10.3892/ol.2020.12203 · Cited by 6

Internal Clocks, mGluR7 and Microtubules: A Primer for the Molecular Encoding of Target Durations in Cerebellar Purkinje Cells and Striatal Medium Spiny Neurons

Yousefzadeh, S. A., Hesslow, G., Shumyatsky, G. P., & Meck, W. H. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00321 · Cited by 6

Non-enzymatic Activity of the α-Tubulin Acetyltransferase αTAT Limits Synaptic Bouton Growth in Neurons

Coombes, C. E., Saunders, H. A. J., Mannava, A. G., Johnson-Schlitz, D. M., Reid, T. A., Parmar, S., McClellan, M., Yan, C. H., Rogers, S. L., Parrish, J. Z., et al. (2020) · Current Biology · doi:10.1016/j.cub.2019.12.022 · Cited by 6

Centrosome and ciliary abnormalities in fetal akinesia deformation sequence human fibroblasts

Jühlen, R., Martinelli, V., Vinci, C., Breckpot, J., & Fahrenkrog, B. (2020) · Scientific Reports · doi:10.1038/s41598-020-76192-1 · Cited by 7

Suppression of alpha-tubulin acetylation potentiates therapeutic efficacy of Eribulin in liver cancer.

Zhong, Y., Wang, C., Wang, Y., Wu, Y., Wang, H., Qiu, S., Hao, M., Wang, Z., Wang, X., Jin, H., et al. (2023) · PubMed Central · Cited by 5

Acetylation of tubulin: A feasible protective target from neurodevelopment to neurodegeneration

Graziella, C., & Cartelli, D. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814037-6.00009-4 · Cited by 5

Macromolecular Crowding Tailors the Microtubule Cytoskeleton Through Tubulin Modifications and Microtubule-Associated ProteinsPreprint

Shen, Y., & Ori-McKenney, K. M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.14.544846 · Cited by 5

Altered Posttranslational Modification of Microtubules Contributes to Disturbed Enterocyte Morphology in Celiac Disease

Stricker, S., Müller, M., Zimmer, K., & Jacob, R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032635 · Cited by 4

The cyto-linker and scaffolding protein “plectin” mis-localization leads to softening of cancer cells

Amiri, A., Dietz, C., Rapp, A. W., Cardoso, M. C., & Stark, R. W. (2023) · Nanoscale · doi:10.1039/d3nr02226a · Cited by 5

Post‐Translational Modifications in Cilia and Ciliopathies

Ran, J., & Zhou, J. (2025) · Advanced Science · doi:10.1002/advs.202416562 · Cited by 3

Mapping of polyglutamylation in tubulins using nanoLC-ESI-MS/MS

McClung, C. M., Chin, H. G., Hansen, U. M., Noren, C. J., Pradhan, S., & Ruse, C. I. (2020) · Analytical Biochemistry · doi:10.1016/j.ab.2020.113761 · Cited by 4

In situ silver nanoparticle development for molecular-specific biological imaging via highly accessible microscopies

Song, D., Song, C. W., Chung, J., Jang, E., Kim, H., Hur, Y., Hur, E., Kim, D., & Chang, J. (2022) · Nanoscale Advances · doi:10.1039/d2na00449f · Cited by 4

ACTB and GAPDH appear at multiple SDS-PAGE positions, thus not suitable as reference genes for determining protein loading in techniques like Western blotting

Zhang, K., Zhang, J., Ding, N., Zellmer, L., Zhao, Y., Liu, S., & Liao, D. J. (2021) · Open Life Sciences · doi:10.1515/biol-2021-0130 · Cited by 4

Spatially Organized Ciliary Beating Compartmentalizes Cerebrospinal Fluid Flow in the Brain and Regulates Ventricular DevelopmentPreprint

Olstad, E. W., Ringers, C., Wens, A., Hansen, J. N., Brandt, C., Yaksi, E., & Jurisch‐Yaksi, N. (2018) · SSRN Electronic Journal · doi:10.2139/ssrn.3199994 · Cited by 4

Collective sperm movement in mammalian reproductive tracts

Hirashima, T., Sound, W. P., & Noda, T. (2024) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2024.12.002 · Cited by 3

Mid-gestational cell-type-specific transcriptomic signatures in the prefrontal and superior temporal cortex in Down syndrome

Niu, R., Xue, L., Tian, X., Huangfu, L., Chen, L., Zhai, C.-Y., Wang, S., Zhao, Y., Gan, Z., Qin, H.-Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-66109-9 · Cited by 3

Antibody-Free Targeted Proteomics Assay for Absolute Measurement of α-Tubulin Acetylation

Shah, A. K., Wali, G., Sue, C. M., Mackay‐Sim, A., & Hill, M. M. C. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c01683 · Cited by 3

Mathematical modeling of the microtubule detyrosination/tyrosination cycle for cell-based drug screening design

Grignard, J., Lamamy, V., Vermersch, E., Delagrange, P., Stéphan, J.-P., Dorval, T., & Fages, F. (2022) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1010236 · Cited by 4

Fluorescence correlation spectroscopy reveals the dynamics of kinesins interacting with organelles during microtubule-dependent transport in cells

Rossi, M. C. D., Bardeci, N. G., Álvarez, Y. D., Mocskos, E., Romero, J. J., Bruno, L., Wetzler, D. E., & Levi, V. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118572 · Cited by 3

MFN2-dependent recruitment of ATAT1 coordinates mitochondria motility with alpha-tubulin acetylation and is disrupted in CMT2APreprint

Kumar, A., Larrea, D., Pero, M. E., Infante, P., Conenna, M., Shin, G. J.-E., Grueber, W. B., Marcotullio, L. D., Área-Gómez, E., & Bartolini, F. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.15.532838 · Cited by 3

A preliminary study on the mechanism of VASH2 in childhood medulloblastoma

Liu, W., Fu, Y., Wang, M., Zhao, J., Chen, J., Wang, Y., & Qin, H. (2023) · Scientific Reports · doi:10.1038/s41598-023-42869-6 · Cited by 2

Design, synthesis and biological activity of tubulin inhibitors based on the structure of deoxypodophyllotoxin

Zhang, M., Zhao, B., Leng, J., Zhu, L., Ning, M., Cao, T.-J., Wu, J., Zhang, C., Li, D., Wang, K., et al. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.108783 · Cited by 2

Pronucleotide Probes Reveal a Diverging Specificity for AMPylation vs UMPylation of Human and Bacterial Nucleotide Transferases

Mostert, D., Bubeneck, W. A., Rauh, T., Kielkowski, P., Itzen, A., Jung, K., & Sieber, S. A. (2024) · Biochemistry · doi:10.1021/acs.biochem.3c00568 · Cited by 2

Tubulin targeting agents and their implications in non-cancer disease management

Lal, S., & Snape, T. J. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104338 · Cited by 2

Moteurs moléculaires et microtubules : relation libre, imposée ou sélective ?

Mallet, A., & Bastin, P. (2019) · médecine/sciences · doi:10.1051/medsci/2019062 · Cited by 2

Tubulin acetylation governs organelle remodeling and lysosomal reformation during neuronal differentiationPreprint

Hsu, C.-H., Kinrade, A. J., Zanellati, M. C., & Cohen, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.13.705749 · Cited by 2

Mitochondrial brain proteome acetylation levels and behavioural responsiveness to amphetamine are altered in mice lacking Sirt3

Sidorova‐Darmos, E., Fallah, M. S., Logan, R., Cheng, L., & Eubanks, J. H. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.948387 · Cited by 1

The Roles of Microtubule-Associated Protein 4 in Wound Healing and Human Diseases

Chen, Q., Zhang, J., Song, Z., & Huang, Y. (2023) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2804076 · Cited by 1

What Are the Fitness Costs of Centromere Drive?

Pan, B., & Akera, T. (2025) · Springer eBooks · doi:10.1007/978-3-031-97173-0_3 · Cited by 1

Prognostic, diagnostic and therapeutic value of the cancer tubulin code

Vilela, C., Gomes-Andrade, D., Silva, S. D. R., & Maiato, H. (2026) · Cancer and Metastasis Reviews · doi:10.1007/s10555-026-10347-w · Cited by 1

Towards a systems-level view of the microtubule cytoskeleton and its functions in physiology and disease

Janke, C., Akhmanova, A. S., Bartolini, F., Bodakuntla, S., Bene, F. D., Hamel, V., Mitchison, T. J., Müller‐Reichert, T., Nédélec, F., Nogales, E., et al. (2026) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-026-01011-w · Cited by 1

The TUBA1B–G3BP2 Axis Sustains p65 Transcriptional Activity to Promote Hepatocellular Carcinoma Progression

Lin, F., Lin, H., Yu, J., Ge, C., Mao, L., Zhang, S.-H., Jin, Y.-Z., Wu, Y.-Y., Chen, T.-Y., Li, J.-J., et al. (2026) · Advancement of science · doi:10.1002/advs.77502 · Cited by 1

The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylationPreprint

Cummings, S. W., Li, Y., Spector, J. O., Kim, C., & Roll‐Mecak, A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.31.587457 · Cited by 1

The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylationPreprint

Cummings, S. W., Li, Y., Spector, J. O., Kim, C., & Roll‐Mecak, A. (2024) · eLife · doi:10.7554/elife.98040 · Cited by 1

Knockdown of TTLL1 reduces Aβ-induced TAU pathology in human iPSC-derived cortical neuronsPreprint

Kabbani, M. A. A., Köhler, L., Wied, T., Adam, D., Klimek, J., & Zempel, H. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.19.624324 · Cited by 1

The tubulin poly-glutamylase complex, TPGC, is required for phosphatidyl inositol homeostasis and cilium assembly and maintenancePreprint

Badarudeen, B., Chiang, H.-J., Collado, L., Wang, L., Sánchez, I., & Dynlacht, B. D. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.03.641315 · Cited by 1

Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling

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

Regulation of KIF1A motility via polyglutamylation of tubulin C-terminal tailsPreprint

Lessard, D. V., Zinder, O. J., Hotta, T., Verhey, K. J., Ohi, R., & Berger, C. L. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/410860

ACTB and GAPDH proteins appear at multiple positions of SDS-PAGE and may not be suitable for serving as reference genes for the protein level determination in such techniques as Western blottingPreprint

He, Y., Zhang, J., Qu, J., Zellmer, L., Zhao, Y., Liu, S., Huang, H., & Liao, D. J. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.05.978494

Sirtuin signaling in hematologic malignancies

Denu, R. A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822467-0.00012-7

Transactive response DNA-binding Protein (TDP-43) regulates early HIV-1 entry and infectionPreprint

Cabrera-Rodríguez, R., Pérez-Yanes, S., González‐Montelongo, R., Lorenzo-Salazar, J. M., Estévez‐Herrera, J., García-Luis, J., Íñigo-Campos, A., Rubio‐Rodríguez, L. A., Muñoz‐Barrera, A., Trujillo‐González, R., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.06.471424

Faculty Opinions recommendation of Genetically encoded live-cell sensor for tyrosinated microtubules.

Matis, M. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.738608587.793579127

The Inhibition Effect of Korean Propolis on Microtubule Polymerization Disassembly Caused by Endoplasmic Reticulum (ER) Stress

Kim, S.-K., Kim, H. Y., Kim, S.-G., Han, S. M., Ryu, S., & Woo, S. O. (2022) · Journal of Apiculture · doi:10.17519/apiculture.2022.04.37.1.75

Childhood-Onset Neurodegeneration with Cerebellar Atrophy Syndrome: Severe Neuronal Degeneration and Cardiomyopathy with Loss of Tubulin Deglutamylase Cytosolic Carboxypeptidase 1

Samur, B. M., Ercan‐Sencicek, A. G., Çağlayan, A. O., Per, H., Gümüş, H., Gümüş, G., & Baykan, A. (2022) · Journal of Pediatric Neurology · doi:10.1055/s-0042-1749669

The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylationPreprint

Cummings, S. W., Li, Y., Spector, J. O., Kim, C., & Roll‐Mecak, A. (2024) · eLife · doi:10.7554/elife.98040.1

The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylationPreprint

Cummings, S. W., Li, Y., Spector, J. O., Kim, C., & Roll‐Mecak, A. (2025) · eLife · doi:10.7554/elife.98040.2

A first step in the gene therapy of tubulin glutamylation disorders

Bougneres, P. F. (2025) · Molecular Therapy · doi:10.1016/j.ymthe.2025.10.025

Tubastatin A attenuates impaired autophagic degradation and promotes myogenic program in skeletal muscle following downhill running

Wang, Z., Lei, B., Hu, J., Ke, Z., Wang, R., & Li, J. (2025) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-025-09717-8

Taxane-Induced Conformational Changes in the Microtubule Lattice Activate GEF-H1-Dependent RhoA SignalingPreprint

Meiring, J. C. M., Mahapatra, V., Gravett, M. S. C., Morren, D., Saunders, H. A. J., Choi, S. R., Jose, A. P., Karhanova, A., Metallidou, I., Moore, A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.20.695343

Regulation of neuronal microtubule-based transport by polyglutamylation

Bodakuntla, S. (2019) · theses.fr (ABES) · doi:10.70675/25a5f130z3b63z4663zb3aez400da5d97e80

Huntingtin functions in the regulation of axonal transport : consequences on neuronal network homeostasis and behavior, in health and disease

Vitet, H. (2020) · theses.fr (ABES) · doi:10.70675/5a5d3bacz6b6ez4a35z9159z6459b40efcdf

Systematic characterization of a large number of Microtubule-Associated Proteins using purification-free TIRF-reconstitution assays

Jijumon, A. S. (2021) · theses.fr (ABES) · doi:10.70675/a91e897dze839z49aezbde4z6f7bfa86d70b

Identification et caractérisation de nouveaux gènes impliqués dans l’assemblage du cil

Carret, A. (2023) · theses.fr (ABES) · doi:10.70675/484f7282z3bfbz4906za6e7zd3957e80fa73

The Role of Intracellular Trafficking in Epithelial Polarity and Cancer

Khalilian, P. (2024) · theses.fr (ABES) · doi:10.70675/e07b96a4z202bz417fzb6f0z7dff79b547c5

Tubulin monoglutamylation is sufficient to rescue the ciliary motility defects in a Chlamydomonas polyglutamylation deficient mutant

Sasaki, R., Oda, T., & Kubo, T. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1857091

Targeting TTLL1 Alleviates Aβ-Induced Microtubule Disruption and TAU Pathology in Human iPSC-Derived Cortical Neurons

Kabbani, M. A. A., Köhler, L., Wied, T., Adam, D., Klimek, J., & Zempel, H. (2026) · Pharmaceutics · doi:10.3390/pharmaceutics18081038 · Cited by 1

Hyperglycemic stress aggravates diabetic retinopathy and nephropathy by promoting cilium disassembly via a deacetylation- and methylation-mediated regulatory mechanism

Ran, J., Wei, C., Yang, Y., Zhang, Y., Guo, G., Ma, N., Yin, L., Fan, H., Li, J., Guo, H., et al. (2026) · PLoS Biology · doi:10.1371/journal.pbio.3003975

USP10 is associated with TUBA1B protein stability, PI3K/AKT phosphorylation changes, and progression of triple-negative breast cancer

Ma, H., Xiao, H., Wang, Y., Li, Y., Zhao, J., Aimaiti, X., Hu, M., & Guo, C. (2026) · Pathology - Research and Practice · doi:10.1016/j.prp.2026.156683

Gain-of-function suppressors restore microtubule dynamics and rescue dominant-negative tubulinopathies

Xu, K., Guo, Z., Ke, J., Chen, Z., Mao, L., Sun, R., Chen, M., Na, J., Xie, S., Zhou, T., et al. (2026) · Nature Cell Biology · doi:10.1038/s41556-026-02066-9

From exercise-associated lactate to the tubulin code: α-tubulin lactylation as a candidate mechanism for poststroke neural remodeling

Guo, J., & Wang, H. (2026) · Frontiers in Physiology · doi:10.3389/fphys.2026.1972705

SnapShot: Functions of Tubulin Posttranslational Modifications

Magiera, M. M., Singh, P., & Janke, C. (2018) · Cell · doi:10.1016/j.cell.2018.05.032 · Cited by 29

Post-translational modifications of tubulin: pathways to functional diversity of microtubules

Song, Y., & Brady, S. T. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.10.004 · Cited by 377

Posttranslational Modifications of Tubulin

Chao, S. K., Yang, C. H., & Horwitz, S. B. (2012) · Humana Press eBooks · doi:10.1007/978-1-61779-788-0_13 · Cited by 21

Post-translational modifications regulate microtubule function

Westermann, S., & Weber, K. K. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1260 · Cited by 716

Tubulin Post-Translational Modifications and Microtubule Dynamics

Włoga, D., Joachimiak, E., & Fabczak, H. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102207 · Cited by 167