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Axonal transport: Driving synaptic function

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Much More Than a Scaffold: Cytoskeletal Proteins in Neurological Disorders

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The Tubulin Code, from Molecules to Health and Disease

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The Mechanism of Tubulin Assembly into Microtubules: Insights from Structural Studies

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Cardiac microtubules in health and heart disease

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The Tubulin Detyrosination Cycle: Function and Enzymes

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Microtubules and cardiovascular diseases: insights into pathology and therapeutic strategies

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MARK4 controls ischaemic heart failure through microtubule detyrosination

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Tubulin post‐translational modifications control neuronal development and functions

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Proteomic and Functional Studies Reveal Detyrosinated Tubulin as Treatment Target in Sarcomere Mutation-Induced Hypertrophic Cardiomyopathy

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The centrosome protein AKNA regulates neurogenesis via microtubule organization

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Detyrosinated microtubules spatially constrain lysosomes facilitating lysosome-autophagosome fusion

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Time-resolved proteomics profiling of the ciliary Hedgehog response

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Microtubule acetylation but not detyrosination promotes focal adhesion dynamics and astrocyte migration

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α-tubulin tail modifications regulate microtubule stability through selective effector recruitment, not changes in intrinsic polymer dynamics

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Post-translational Modifications of the Protein Termini

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The Tubulin Code in Mitosis and Cancer

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The detyrosination/re-tyrosination cycle of tubulin and its role and dysfunction in neurons and cardiomyocytes

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Posttranslational modification of microtubules by the MATCAP detyrosinase

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Structural basis of tubulin detyrosination by vasohibins

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Molecular basis of vasohibins-mediated detyrosination and its impact on spindle function and mitosis

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Tubulin tyrosination regulates synaptic function and is disrupted in Alzheimer’s disease

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Microtubule acetylation dyshomeostasis in Parkinson’s disease

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Defective tubulin detyrosination causes structural brain abnormalities with cognitive deficiency in humans and mice

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The tubulin code in neuronal polarity

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Structural basis of tubulin detyrosination by the vasohibin–SVBP enzyme complex

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Posttranslational modifications of the cytoskeleton

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Distinct roles of α‐ and β‐tubulin polyglutamylation in controlling axonal transport and in neurodegeneration

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Purification of tubulin with controlled post-translational modifications by polymerization–depolymerization cycles

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Intrinsic and Extrinsic Factors Affecting Microtubule Dynamics in Normal and Cancer Cells

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Tubulin heterogeneity regulates functions and dynamics of microtubules and plays a role in the development of drug resistance in cancer

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Cardiomyocyte Microtubules: Control of Mechanics, Transport, and Remodeling

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The cytoskeleton and connected elements in bone cell mechano-transduction

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The microtubule cytoskeleton: An old validated target for novel therapeutic drugs

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Combinatorial and antagonistic effects of tubulin glutamylation and glycylation on katanin microtubule severing

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Mix and (mis-)match – The mechanosensing machinery in the changing environment of the developing, healthy adult and diseased heart

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α-Tubulin detyrosination impairs mitotic error correction by suppressing MCAK centromeric activity

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Pathogenic role of delta 2 tubulin in bortezomib-induced peripheral neuropathy

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More than Microtubules: The Structure and Function of the Subpellicular Array in Trypanosomatids

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Depletion of Vasohibin 1 Speeds Contraction and Relaxation in Failing Human Cardiomyocytes

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Precise control of microtubule disassembly in living cells

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The centriolar tubulin code

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Don’t you forget about me(gakaryocytes)

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Current Technologies Unraveling the Significance of Post-Translational Modifications (PTMs) as Crucial Players in Neurodegeneration

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Septin filament coalignment with microtubules depends on SEPT9_i1 and tubulin polyglutamylation, and is an early feature of acquired cell resistance to paclitaxel

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Dissecting the role of the tubulin code in mitosis

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Cryo-EM structure of VASH1-SVBP bound to microtubules

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Direct and indirect effects of tubulin post-translational modifications on microtubule stability: Insights and regulations

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The Role of Spastin in Axon Biology

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Cellular cartography: Towards an atlas of the neuronal microtubule cytoskeleton

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Leishmania-infected macrophages release extracellular vesicles that can promote lesion development

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Crystal structure of VASH1-SVBP complex bound with EpoY

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Insights on the Role of α- and β-Tubulin Isotypes in Early Brain Development

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Control of motor landing and processivity by the CAP-Gly domain in the KIF13B tail

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Chronic Activation of Tubulin Tyrosination Improves Heart Function

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PTEN suppresses axon outgrowth by down-regulating the level of detyrosinated microtubules

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Genetically encoded live-cell sensor for tyrosinated microtubules

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The chaperonin CCT controls T cell receptor–driven 3D configuration of centrioles

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Loss of function of SVBP leads to autosomal recessive intellectual disability, microcephaly, ataxia, and hypotonia

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Vasohibin‐2 plays an essential role in metastasis of pancreatic ductal adenocarcinoma

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Parthenolide Destabilizes Microtubules by Covalently Modifying Tubulin

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Tubulin engineering by semi-synthesis reveals that polyglutamylation directs detyrosination

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Crystal structure of the tubulin tyrosine carboxypeptidase complex VASH1–SVBP

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Evolutionary Divergence of Enzymatic Mechanisms for Tubulin Detyrosination

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The tubulin code in mammalian sperm development and function

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Microtubule detyrosination by VASH1/SVBP is regulated by the conformational state of tubulin in the lattice

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Mechanoactivation of NOX2-generated ROS elicits persistent TRPM8 Ca 2+ signals that are inhibited by oncogenic KRas

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MACF1 controls skeletal muscle function through the microtubule-dependent localization of extra-synaptic myonuclei and mitochondria biogenesis

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Crosstalk between acetylation and the tyrosination/detyrosination cycle of α-tubulin in Alzheimer’s disease

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Microtubule-Associated Proteins with Regulatory Functions by Day and Pathological Potency at Night

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α-TubK40me3 is required for neuronal polarization and migration by promoting microtubule formation

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Structural basis of tubulin detyrosination by VASH2/SVBP heterodimer

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Disruption of tubulin-alpha4a polyglutamylation prevents aggregation of hyper-phosphorylated tau and microglia activation in mice

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A family of carboxypeptidases catalyzing α- and β-tubulin tail processing and deglutamylation

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The Tubulin Code and Tubulin-Modifying Enzymes in Autophagy and Cancer

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Microtubule remodelling as a driving force of axon guidance and pruning

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Endogenous Antiangiogenic Factors in Chronic Kidney Disease: Potential Biomarkers of Progression

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Adenosine kinase attenuates cardiomyocyte microtubule stabilization and protects against pressure overload-induced hypertrophy and LV dysfunction

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Tubulin and Tubulin Posttranslational Modifications in Alzheimer’s Disease and Vascular Dementia

Santiago-Mujika, E., Luthi‐Carter, R., Giorgini, F., Kalaria, R. N., & Mukaetova-Ladinska, E. B. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.730107 · Cited by 26

Microtubule detyrosination drives symmetry breaking to polarize cells for directed cell migration

Lavrsen, K., Rajendraprasad, G., Leda, M., Eibes, S., Vitiello, E., Katopodis, V., Goryachev, A. B., & Barišić, M. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2300322120 · Cited by 28

EML2-S constitutes a new class of proteins that recognizes and regulates the dynamics of tyrosinated microtubules

Hotta, T., McAlear, T. S., Yang, Y., Higaki, T., Haynes, S. E., Nesvizhskii, A. I., Sept, D., Verhey, K. J., Bechstedt, S., & Ohi, R. (2022) · Current Biology · doi:10.1016/j.cub.2022.07.027 · Cited by 34

VASH1–SVBP and VASH2–SVBP generate different detyrosination profiles on microtubules

Ramírez‐Ríos, S., Choi, S. R., Sanyal, C., Blum, T. B., Bosc, C., Krichen, F., Denarier, É., Soleilhac, J.-M., Blot, B., Janke, C., et al. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202205096 · Cited by 28

The emerging role of tubulin posttranslational modifications in cilia and ciliopathies

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The metaphase spindle at steady state – Mechanism and functions of microtubule poleward flux

Barišić, M., Rajendraprasad, G., & Steblyanko, Y. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.05.016 · Cited by 27

Vasohibin inhibition improves myocardial relaxation in a rat model of heart failure with preserved ejection fraction

Eaton, D., Lee, B. W., Caporizzo, M. A., Iyengar, A., Chen, C. Y., Uchida, K., Marcellin, G., Lannay, Y., Vite, A., Bedi, K. C., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adm8842 · Cited by 25

Tubulin post-translational modifications in meiosis

Akera, T. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.11.014 · Cited by 24

Microtubule‐associated proteins and enzymes modifying tubulin

Peng, N., & Nakamura, F. (2023) · Cytoskeleton · doi:10.1002/cm.21748 · Cited by 23

CSAP Acts as a Regulator of TTLL-Mediated Microtubule Glutamylation

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Microtubule function and dysfunction in the nervous system

Jang, E., Choi, H., & Hur, E. (2024) · Molecules and Cells · doi:10.1016/j.mocell.2024.100111 · Cited by 24

Augmin-dependent microtubule self-organization drives kinetochore fiber maturation in mammals

Almeida, A. C., Soares-de-Oliveira, J., Drpic, D., Cheeseman, L. P., Damas, J., Lewin, H. A., Larkin, D. M., Aguiar, P., Pereira, A. J., & Maiato, H. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110610 · Cited by 23

Renal tubular injury exacerbated by vasohibin-1 deficiency in a murine cisplatin-induced acute kidney injury model

Tanimura, S., Tanabe, K., Miyake, H., Masuda, K., Tsushida, K., Morioka, T., Sugiyama, H., Sato, Y., & Wada, J. (2019) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00045.2019 · Cited by 23

Stereoselective total synthesis of parthenolides indicates target selectivity for tubulin carboxypeptidase activity

Freund, R. R. A., Gobrecht, P., Rao, Z., Gerstmeier, J., Schlosser, R., Görls, H., Werz, O., Fischer, D., & Arndt, H. (2019) · Chemical Science · doi:10.1039/c9sc01473j · Cited by 23

Tubulin carboxypeptidase activity of vasohibin-1 inhibits angiogenesis by interfering with endocytosis and trafficking of pro-angiogenic factor receptors

Kobayashi, M., Wakabayashi, I., Suzuki, Y., Fujiwara, K., Nakayama, M., Watabe, T., & Sato, Y. (2020) · Angiogenesis · doi:10.1007/s10456-020-09754-6 · Cited by 23

Fbxo45 Binds SPRY Motifs in the Extracellular Domain of N-Cadherin and Regulates Neuron Migration during Brain Development

Na, Y., Calvo-Jiménez, E., Kon, E., Cao, H., Jossin, Y., & Cooper, J. A. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00539-19 · Cited by 21

Tubulin carboxypeptidase identity revealed

Hurtley, S. M. (2017) · Science · doi:10.1126/science.358.6369.1397-r

Structural basis of tubulin detyrosination by the vasohibin–SVBP enzyme complex

Wang, N., Bosc, C., Choi, S. R., Boulan, B., Peris, L., Olieric, N., Bao, H., Krichen, F., Chen, L., Andrieux, A., et al. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0241-y · Cited by 61

Vasohibins encode tubulin detyrosinating activity

Nieuwenhuis, J., Adamopoulos, A., Bleijerveld, O. B., Mazouzi, A., Stickel, E., Celie, P., Altelaar, M., Knipscheer, P., Perrakis, A., Blomen, V. A., et al. (2017) · Science · doi:10.1126/science.aao5676 · Cited by 266

Structural basis of tubulin detyrosination by vasohibins

Li, F., Hu, Y., Qi, S., Luo, X., & Yu, H. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0242-x · Cited by 68

Molecular basis of vasohibins-mediated detyrosination and its impact on spindle function and mitosis

Liao, S., Rajendraprasad, G., Wang, N., Eibes, S., Gao, J., Yu, H., Wu, G., Tu, X., Huang, H., Barišić, M., et al. (2019) · Cell Research · doi:10.1038/s41422-019-0187-y · Cited by 71