Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation
Open accessAbstract
Tubulin carboxypeptidase identity revealed: Enzymes of the α-tubulin detyrosination/tyrosination cycle create landmarks on microtubules that are essential for their multiple cellular functions and are altered in disease. Tubulin carboxypeptidases (TCPs) responsible for detyrosination have remained elusive for 40 years (see the Perspective by Akhmanova and Maiato). Aillaud et al. identified vasohibins as enzymes that perform the TCP function and found that their small interacting partner SBVP was essential for their activity. Vasohibin/SVBP complexes were involved in neuron polarization and brain cortex development. The authors also developed an inhibitor targeting this family of enzymes. Using a completely different strategy, Nieuwenhuis et al. also showed that vasohibins can remove the C-terminal tyrosine of α-tubulin. Science , this issue p. 1448 , p. 1453 ; see also p. 1381
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Induction of microtubule detyrosination by overexpressing VASH2-SVBP or MATCAP either did not impact the localization of GEF-H1 to microtubules or showed a slight increase in binding.
“Induction of microtubule detyrosination (removal of the C-terminal tyrosine of α-tubulin), another modification associated with microtubule stability 31 , by overexpressing the detyrosinating enzymes VASH2-SVBP or MATCAP 56-58 , either did not impact the localization of GEF-H1 to microtubules or showed a slight increase in binding (Extended Data Fig. 4b-e).”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [56]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Engineering and characterization of a superfolder green fluorescent protein
Pédelacq, J. D., Cabantous, S., Tran, T. H., Terwilliger, T. C., & Waldo, G. S. (2005) · Nature Biotechnology · doi:10.1038/nbt1172 · Cited by 2,295 · see citing works
3D reconstruction of histological sections: Application to mammary gland tissue
Arganda‐Carreras, I., Fernández‐González, R., Muñoz‐Barrutia, A., & Ortíz-de-Solórzano, C. (2010) · Microscopy Research and Technique · doi:10.1002/jemt.20829 · Cited by 715 · see citing works
Tubulin tyrosination navigates the kinesin-1 motor domain to axons
Konishi, Y., & Setou, M. (2009) · Nature Neuroscience · doi:10.1038/nn.2314 · Cited by 415 · see citing works
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 · see citing works
Self-citationPeris, L., Théry, M., Fauré, J., Saoudi, Y., Lafanéchère, L., Chilton, J. K., Gordon‐Weeks, P. R., Galjart, N., Bornens, M., Wordeman, L. G., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512058 · Cited by 347 · see citing works
Self-citationDetyrosinated 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 · see citing works
A vital role of tubulin-tyrosine-ligase for neuronal organization
Erck, C., Peris, L., Andrieux, A., Meissirel, C., Gruber, A. D., Vernet, M., Schweitzer, A., Saoudi, Y., Pointu, H., Bosc, C., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409626102 · Cited by 295 · see citing works
Self-citationMicrotubule detyrosination guides chromosomes during mitosis
Barišić, M., Sousa, R. S. E., Tripathy, S. K., Magiera, M. M., Zaytsev, A. V., Pereira, A. L., Janke, C., Grishchuk, E. L., & Maiato, H. (2015) · Science · doi:10.1126/science.aaa5175 · Cited by 253 · see citing works
Detyrosinated microtubules modulate mechanotransduction in heart and skeletal muscle
Kerr, J. P., Robison, P., Shi, G., Bogush, A. I., Kempema, A., Hexum, J. K., Becerra, N., Harki, D. A., Martin, S. S., Raiteri, R., et al. (2015) · Nature Communications · doi:10.1038/ncomms9526 · Cited by 210 · see citing works
Lafanéchère, L., Manier, M., Trigault, N., Pirollet, F., Mazarguil, H., & Job, D. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.6.1529 · Cited by 202 · see citing works
Preferential action of a brain detyrosinolating carboxypeptidase on polymerized tubulin.
Kumar, N., & Flavin, M. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69014-9 · Cited by 188 · see citing works
Hallak, M. E., Rodriguez, J. A., Barra, H. S., & Caputto, R. (1977) · FEBS Letters · doi:10.1016/0014-5793(77)80968-x · Cited by 158 · see citing works
Whipple, R. A., Matrone, M. A., Cho, E. H., Balzer, E. M., Vitolo, M. I., Yoon, J. R., Ioffe, O. B., Tuttle, K. C., Yang, J., & Martin, S. S. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-4613 · Cited by 156 · see citing works
Posttranslational tyrosination/detyrosination of tubulin
Barra, H. S., ARCE, C. A., & Argaraña, C. E. (1988) · Molecular Neurobiology · doi:10.1007/bf02935343 · Cited by 154 · see citing works
Parthenolide Inhibits Tubulin Carboxypeptidase Activity
Fonrose, X., Ausseil, F., Soleilhac, E., Masson, V., David, B., Pouny, I., Cintrat, J., Rousseau, B., Barette, C., Massiot, G., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3732 · Cited by 125 · see citing works
The vasohibin family: a novel family for angiogenesis regulation
Sato, Y. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs128 · Cited by 111 · see citing works
Suppression of tubulin tyrosine ligase during tumor growth
Lafanéchère, L., Courtay, C., Kawakami, T., Jacrot, M., Rüdiger, M., Wehland, J., Job, D., & Margolis, R. L. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.2.171 · Cited by 110 · see citing works
Barnat, M., Friec, J. L., Benstaali, C., & Humbert, S. (2016) · Neuron · doi:10.1016/j.neuron.2016.11.035 · Cited by 105 · see citing works
Self-citationShibuya, T., Watanabe, K., Yamashita, H., Shimizu, K., Miyashita, H., Abé, M., Moriya, T., Ohta, H., Sonoda, H., Shimosegawa, T., et al. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000216747.66660.26 · Cited by 99 · see citing works
Proteomic Analysis of the Multimeric Nuclear Egress Complex of Human Cytomegalovirus
Milbradt, J., Kraut, A., Hutterer, C., Sonntag, E., Schmeiser, C., Ferro, M., Wagner, S., Roviš, T. L., Claus, C., Pinkert, S., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.035782 · Cited by 93 · see citing works
Self-citationTubulinyl‐tyrosine Carboxypeptidase from Chicken Brain: Properties and Partial Purification
Argaraña, C. E., Barra, H. S., & Caputto, R. (1980) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1980.tb04628.x · Cited by 90 · see citing works
Promotion of Functional Nerve Regeneration by Inhibition of Microtubule Detyrosination
Gobrecht, P., Andreadaki, A., Diekmann, H., Heskamp, A., Leibinger, M., & Fischer, D. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.4486-15.2016 · Cited by 77 · see citing works
Mass Spectrometry Analysis of C-Terminal Posttranslational Modifications of Tubulins
Redeker, V. (2010) · Methods in cell biology · doi:10.1016/s0091-679x(10)95006-1 · Cited by 76 · see citing works
Suppression of nuclear oscillations in Saccharomyces cerevisiae expressing Glu tubulin
Badin-Larçon, A.-C., Boscheron, C., Soleilhac, J.-M., Piel, M., Mann, C., Denarier, É., Fourest‐Lieuvin, A., Lafanéchère, L., Bornens, M., & Job, D. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307917101 · Cited by 76 · see citing works
Tubulin Tyrosination Is Required for the Proper Organization and Pathfinding of the Growth Cone
Marcos, S., Moreau, J., Backer, S., Job, D., Andrieux, A., & Bloch‐Gallego, E. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005405 · Cited by 75 · see citing works
Self-citationA revised nomenclature for the human and rodent α-tubulin gene family
Khodiyar, V., Maltais, L. J., Sneddon, K. M. B., Smith, J. R., Shimoyama, M. E., Cabral, F., Dumontet, C., Dutcher, S. K., Harvey, R. J., Lafanéchère, L., et al. (2007) · Genomics · doi:10.1016/j.ygeno.2007.04.008 · Cited by 72 · see citing works
Isolation of a small vasohibin-binding protein (SVBP) and its role in vasohibin secretion
Suzuki, Y., Kobayashi, M., Miyashita, H., Ohta, H., Sonoda, H., & Sato, Y. (2010) · Journal of Cell Science · doi:10.1242/jcs.067538 · Cited by 65 · see citing works
Evidence for new C-terminally truncated variants of α- and β-tubulins
Aillaud, C., Bosc, C., Saoudi, Y., Denarier, É., Peris, L., Sago, L., Taulet, N., Cieren, A., Tort, O., Magiera, M. M., et al. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-03-0137 · Cited by 64 · see citing works
Self-citationRamirez-Rios, S., Denarier, E., Prezel, E., Vinit, A., Stoppin-Mellet, V., Devred, F., Barbier, P., Peyrot, V., Sayas, C. L., Ávila, J., et al. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-01-0029 · Cited by 61 · see citing works
Self-citationSmall-molecule inhibition of a depalmitoylase enhances Toxoplasma host-cell invasion
Child, M. A., Hall, C. I., Beck, J. R., Ofori, L. O., Albrow, V. E., Garland, M., Bowyer, P. W., Bradley, P. J., Powers, J. C., Boothroyd, J. C., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1315 · Cited by 60 · see citing works
Self-citationPost-translational modifications of cardiac tubulin during chronic heart failure in the rat
Belmadani, S., Poüs, C., Ventura‐Clapier, R., Fischmeister, R., & Méry, P. (2002) · Molecular and Cellular Biochemistry · doi:10.1023/a:1016554104209 · Cited by 43 · see citing works
Sánchez‐Pulido, L., & Ponting, C. P. (2016) · Bioinformatics · doi:10.1093/bioinformatics/btv761 · Cited by 41 · see citing works
Rovini, A. M. F., GAUTHIER, G. F., Bergès, R., Kruczynski, A., Braguer, D., & Honoré, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065694 · Cited by 33 · see citing works
On the Mechanism of Turnover of the Carboxy-Terminal Tyrosine of the Alpha Chain of Tubulin
Deanin, G. G., Preston, S. F., Hanson, R. K., & Gordon, M. W. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb04786.x · Cited by 24 · see citing works
Expression pattern of Vasohibin during chick development
Nimmagadda, S., Geetha‐Loganathan, P., Pröls, F., Scaal, M., Christ, B., & Huang, R. (2007) · Developmental Dynamics · doi:10.1002/dvdy.21134 · Cited by 21 · see citing works
Cap-Gly Proteins at Microtubule Plus Ends: Is EB1 Detyrosination Involved?
Bosson, A., Soleilhac, J.-M., Valiron, O., Job, D., Andrieux, A., & Moutin, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033490 · Cited by 10 · see citing works
Self-citationDitamo, Y., Dentesano, Y. M., Purro, S. A., Arce, C. A., & Bisig, C. G. (2016) · Scientific Reports · doi:10.1038/srep38140 · Cited by 9 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The tubulin code and its role in controlling microtubule properties and functions
Janke, C., & Magiera, M. M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0214-3 · Cited by 956 · 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
The Tubulin Code in Microtubule Dynamics and Information Encoding
Roll‐Mecak, A. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.06.008 · Cited by 307 · see citing works
Wang, H., Deng, Q., Lv, Z., Ling, Y., Hou, X., Chen, Z., Dinglin, X.-X., Ma, S., Li, D., Wu, Y., et al. (2019) · Molecular Cancer · doi:10.1186/s12943-019-1108-x · Cited by 215 · see citing works
RetractedAdvances in chemistry and bioactivity of parthenolide
Freund, R. R. A., Gobrecht, P., Fischer, D., & Arndt, H. (2019) · Natural Product Reports · doi:10.1039/c9np00049f · Cited by 191 · see citing works
Tubulin Posttranslational Modifications and Emerging Links to Human Disease
Magiera, M. M., Singh, P., Gadadhar, S., & Janke, C. (2018) · Cell · doi:10.1016/j.cell.2018.05.018 · Cited by 169 · see citing works
Much More Than a Scaffold: Cytoskeletal Proteins in Neurological Disorders
Muñoz-Lasso, D. C., Mateo, C. R., Pallardó, F. V., & González‐Cabo, P. (2020) · Cells · doi:10.3390/cells9020358 · Cited by 129 · see citing works
The Tubulin Code, from Molecules to Health and Disease
McKenna, E. D., Sarbanes, S. L., Cummings, S. W., & Roll‐Mecak, A. (2023) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-030123-032748 · Cited by 115 · see citing works
The Mechanism of Tubulin Assembly into Microtubules: Insights from Structural Studies
Knossow, M., Campanacci, V., Khodja, L. A., & Gigant, B. (2020) · iScience · doi:10.1016/j.isci.2020.101511 · Cited by 122 · see citing works
Cardiac microtubules in health and heart disease
Caporizzo, M. A., Chen, C. Y., & Prosser, B. L. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219868960 · Cited by 115 · see citing works
The Tubulin Detyrosination Cycle: Function and Enzymes
Nieuwenhuis, J., & Brummelkamp, T. R. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.08.003 · Cited by 108 · see citing works
Microtubules and cardiovascular diseases: insights into pathology and therapeutic strategies
Wu, Q., Wang, Y., Liu, J., Guan, X., Chang, X., Liu, Z., & Liu, R. (2024) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2024.106650 · Cited by 112 · see citing works
MARK4 controls ischaemic heart failure through microtubule detyrosination
Yu, X., Chen, X., Amrute‐Nayak, M., Allgeyer, E. S., Zhao, A., Chenoweth, H., Clément, M., Harrison, J. E., Doreth, C., Sirinakis, G., et al. (2021) · Nature · doi:10.1038/s41586-021-03573-5 · Cited by 105 · see citing works
Microtubules Increase Diastolic Stiffness in Failing Human Cardiomyocytes and Myocardium
Caporizzo, M. A., Chen, C. Y., Bedi, K., Margulies, K. B., & Prosser, B. L. (2020) · Circulation · doi:10.1161/circulationaha.119.043930 · Cited by 104 · see citing works
Tubulin post‐translational modifications control neuronal development and functions
Moutin, M., Bosc, C., Peris, L., & Andrieux, A. (2020) · Developmental Neurobiology · doi:10.1002/dneu.22774 · Cited by 97 · see citing works
Self-citationSchuldt, M., Pei, J., Harakaľová, M., Dorsch, L. M., Schlossarek, S., Mokrý, M., Knol, J. C., Pham, T. V., Schelfhorst, T., Piersma, S. R., et al. (2021) · Circulation Heart Failure · doi:10.1161/circheartfailure.120.007022 · Cited by 102 · see citing works
Self-citationThe centrosome protein AKNA regulates neurogenesis via microtubule organization
Ortega, G. C., Falk, S., Johansson, P. A., Peyre, E., Broix, L., Sahu, S. K., Hirst, W. G., Schlichthaerle, T., Romero, C. D. J., Draganova, K., et al. (2019) · Nature · doi:10.1038/s41586-019-0962-4 · 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
Time-resolved proteomics profiling of the ciliary Hedgehog response
May, E. A., Kalocsay, M., d'Auriac, I. G., Schuster, P. S., Gygi, S. P., Nachury, M. V., & Mick, D. U. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202007207 · Cited by 86 · see citing works
Bance, B., Seetharaman, S., Leduc, C., Boëda, B., & Etienne‐Manneville, S. (2019) · Journal of Cell Science · doi:10.1242/jcs.225805 · Cited by 90 · see citing works
Chen, J., Kholina, E. G., Szyk, A., Fedorov, V. A., Kovalenko, I. B., Гудимчук, Н. Б., & Roll‐Mecak, A. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.05.005 · Cited by 95 · see citing works
Post-translational Modifications of the Protein Termini
Chen, L., & Kashina, A. S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.719590 · Cited by 89 · see citing works
The Tubulin Code in Mitosis and Cancer
Lopes, D., & Maiato, H. (2020) · Cells · doi:10.3390/cells9112356 · Cited by 84 · see citing works
Sanyal, C., Pietsch, N., Ramírez‐Ríos, S., Peris, L., Carrier, L., & Moutin, M. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.12.006 · Cited by 80 · see citing works
Self-citationPosttranslational 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
Self-citationStructural 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 · see citing works
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 · see citing works
Tubulin tyrosination regulates synaptic function and is disrupted in Alzheimer’s disease
Peris, L., Parato, J., Qu, X., Soleilhac, J.-M., Lanté, F., Kumar, A., Pero, M. E., Hernández, J. M., Corrao, C., Falivelli, G., et al. (2021) · Brain · doi:10.1093/brain/awab436 · Cited by 65 · see citing works
Self-citationMicrotubule acetylation dyshomeostasis in Parkinson’s disease
Naren, P., Khan, S. S., Tryphena, K. P., Vora, L. K., Srivastava, S., Singh, S. B., & Khatri, D. K. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00354-0 · Cited by 63 · see citing works
Pagnamenta, A. T., Heemeryck, P., Martin, H. C., Bosc, C., Peris, L., Uszynski, I., Gory‐Fauré, S., Couly, S., Deshpande, C., Siddiqui, A. U., et al. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz186 · Cited by 64 · see citing works
Self-citationThe tubulin code in neuronal polarity
Park, J. H., & Roll‐Mecak, A. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.03.001 · Cited by 61 · see citing works
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 · see citing works
Self-citationPosttranslational modifications of the cytoskeleton
MacTaggart, B., & Kashina, A. S. (2021) · Cytoskeleton · doi:10.1002/cm.21679 · Cited by 61 · see citing works
Bodakuntla, S., Yuan, X., Genova, M., Gadadhar, S., Leboucher, S., Birling, M., Klein, D., Martini, R., Janke, C., & Magiera, M. M. (2021) · The EMBO Journal · doi:10.15252/embj.2021108498 · Cited by 56 · see citing works
Souphron, J., Bodakuntla, S., Jijumon, A. S., Lakisic, G., Gautreau, A. M., Janke, C., & Magiera, M. M. (2019) · Nature Protocols · doi:10.1038/s41596-019-0153-7 · Cited by 66 · see citing works
Intrinsic and Extrinsic Factors Affecting Microtubule Dynamics in Normal and Cancer Cells
Borys, F., Joachimiak, E., Krawczyk, H., & Fabczak, H. (2020) · Molecules · doi:10.3390/molecules25163705 · Cited by 55 · see citing works
Prassanawar, S. S., & Panda, D. (2019) · Biochemical Journal · doi:10.1042/bcj20190123 · Cited by 55 · see citing works
Cardiomyocyte Microtubules: Control of Mechanics, Transport, and Remodeling
Uchida, K., Scarborough, E. A., & Prosser, B. L. (2021) · Annual Review of Physiology · doi:10.1146/annurev-physiol-062421-040656 · Cited by 59 · see citing works
The cytoskeleton and connected elements in bone cell mechano-transduction
Gould, N. R., Torre, O. M., Leser, J. M., & Stains, J. P. (2021) · Bone · doi:10.1016/j.bone.2021.115971 · Cited by 56 · see citing works
The microtubule cytoskeleton: An old validated target for novel therapeutic drugs
Lafanéchère, L. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.969183 · Cited by 51 · see citing works
Szczęsna, E., Zehr, E. A., Cummings, S. W., Szyk, A., Mahalingan, K. K., Li, Y., & Roll‐Mecak, A. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.10.003 · Cited by 56 · see citing works
Ward, M. J., & Iskratsch, T. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.01.017 · Cited by 51 · see citing works
α-Tubulin detyrosination impairs mitotic error correction by suppressing MCAK centromeric activity
Ferreira, L. T., Orr, B., Rajendraprasad, G., Pereira, A. J., Lemos, C., Lima, J. T., Boldú, C. G., Ferreira, J. G. G., Barišić, M., & Maiato, H. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201910064 · Cited by 52 · see citing works
Pathogenic role of delta 2 tubulin in bortezomib-induced peripheral neuropathy
Pero, M. E., Meregalli, C., Qu, X., Shin, G. J.-E., Kumar, A., Shorey, M., Rolls, M. M., Tanji, K., Brannagan, T. H., Alberti, P., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2012685118 · Cited by 48 · see citing works
More than Microtubules: The Structure and Function of the Subpellicular Array in Trypanosomatids
Sinclair, A. N., & de Graffenried, C. L. (2019) · Trends in Parasitology · doi:10.1016/j.pt.2019.07.008 · Cited by 46 · see citing works
Depletion of Vasohibin 1 Speeds Contraction and Relaxation in Failing Human Cardiomyocytes
Chen, C. Y., Salomon, A. K., Caporizzo, M. A., Curry, S., Kelly, N. A., Bedi, K. C., Bogush, A. I., Krämer, E., Schlossarek, S., Janiak, P., et al. (2020) · Circulation Research · doi:10.1161/circresaha.119.315947 · Cited by 46 · see citing works
Self-citationPrecise control of microtubule disassembly in living cells
Liu, G. Y., Chen, S., Lee, G., Shaiv, K., Chen, P., Cheng, H., Hong, S., Yang, W., Huang, S., Chang, Y., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2021110472 · Cited by 45 · see citing works
Guichard, P., Laporte, M. H., & Hamel, V. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.12.001 · Cited by 44 · see citing works
Don’t you forget about me(gakaryocytes)
Tilburg, J., Becker, I. C., & Italiano, J. E. (2021) · Blood · doi:10.1182/blood.2020009302 · Cited by 43 · see citing works
Zafar, S., Fatima, S. I., Schmitz, M., & Zerr, I. (2024) · Biomolecules · doi:10.3390/biom14010118 · Cited by 42 · see citing works
Targa, B., Klipfel, L., Cantaloube, I., Salameh, J., Benoit, B., Poüs, C., & Baillet, A. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1318-6 · Cited by 42 · see citing works
Dissecting the role of the tubulin code in mitosis
Ferreira, L. T., Figueiredo, A. C., Orr, B., Lopes, D., & Maiato, H. (2018) · Methods in cell biology · doi:10.1016/bs.mcb.2018.03.040 · Cited by 40 · see citing works
Cryo-EM structure of VASH1-SVBP bound to microtubules
Li, F., Li, Y., Ye, X., Gao, H., Shi, Z., Luo, X., Rice, L. M., & Yu, H. (2020) · eLife · doi:10.7554/elife.58157 · Cited by 40 · see citing works
Bär, J., Popp, Y., Bucher, M., & Mikhaylova, M. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119241 · Cited by 40 · see citing works
The Role of Spastin in Axon Biology
Costa, A. C., & Sousa, M. M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.934522 · Cited by 35 · see citing works
Cellular cartography: Towards an atlas of the neuronal microtubule cytoskeleton
Iwanski, M. K., & Kapitein, L. C. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1052245 · Cited by 38 · see citing works
Leishmania-infected macrophages release extracellular vesicles that can promote lesion development
Gioseffi, A., Hamerly, T., Van, K., Zhang, N., Dinglasan, R. R., Yates, P. A., & Kima, P. E. (2020) · Life Science Alliance · doi:10.26508/lsa.202000742 · Cited by 39 · see citing works
Crystal structure of VASH1-SVBP complex bound with EpoY
Li, F., Luo, X., & Yu, H. (2019) · Worldwide Protein Data Bank · doi:10.2210/pdb6ocg/pdb · Cited by 39 · see citing works
Insights on the Role of α- and β-Tubulin Isotypes in Early Brain Development
Tantry, M. S. A., & Santhakumar, K. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03302-1 · Cited by 38 · see citing works
Control of motor landing and processivity by the CAP-Gly domain in the KIF13B tail
Fan, X., & McKenney, R. J. (2023) · Nature Communications · doi:10.1038/s41467-023-40425-4 · Cited by 46 · see citing works
Chronic Activation of Tubulin Tyrosination Improves Heart Function
Pietsch, N., Chen, C. Y., Kupsch, S., Bacmeister, L., Geertz, B., Herrera-Rivero, M., Siebels, B., Voß, H., Krämer, E., Braren, I., et al. (2024) · Circulation Research · doi:10.1161/circresaha.124.324387 · Cited by 37 · see citing works
PTEN suppresses axon outgrowth by down-regulating the level of detyrosinated microtubules
Kath, C., Goñi‐Oliver, P., Müller, R., Schultz, C., Haucke, V., Eickholt, B. J., & Schmoranzer, J. (2018) · PLoS ONE · doi:10.1371/journal.pone.0193257 · Cited by 37 · see citing works
Genetically encoded live-cell sensor for tyrosinated microtubules
Kesarwani, S., Lama, P., Chandra, A., Reddy, P. P., Jijumon, A. S., Bodakuntla, S., Rao, B. M., Janke, C., Das, R., & Sirajuddin, M. (2020) · Journal of Cell Biology · doi:10.1083/jcb.201912107 · Cited by 37 · see citing works
The chaperonin CCT controls T cell receptor–driven 3D configuration of centrioles
Martin-Cofreces, N. B., Chichón, F. J., Calvo, E., Torralba, D., Bustos‐Morán, E., Dosil, S. G., Rojas‐Gómez, A., Bonzón‐Kulichenko, E., López, J. A., Otón, J., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb7242 · Cited by 40 · see citing works
Iqbal, Z., Tawamie, H., Ba, W., Reis, A., Hallak, B. A., Sticht, H., Uebe, S., Kasri, N. N., Riazuddin, S. A., van Bokhoven, H., et al. (2019) · Genetics in Medicine · doi:10.1038/s41436-018-0415-8 · Cited by 33 · see citing works
Vasohibin‐2 plays an essential role in metastasis of pancreatic ductal adenocarcinoma
Iida‐Norita, R., Kawamura, M., Suzuki, Y., Hamada, S., Masamune, A., Furukawa, T., & Sato, Y. (2019) · Cancer Science · doi:10.1111/cas.14041 · Cited by 36 · see citing works
Parthenolide Destabilizes Microtubules by Covalently Modifying Tubulin
Hotta, T., Haynes, S. E., Blasius, T. L., Gebbie, M., Eberhardt, E. L., Sept, D., Cianfrocco, M. A., Verhey, K. J., Nesvizhskii, A. I., & Ohi, R. (2020) · Current Biology · doi:10.1016/j.cub.2020.11.055 · Cited by 35 · see citing works
Tubulin engineering by semi-synthesis reveals that polyglutamylation directs detyrosination
Ebberink, E. H. T. M., Fernandes, S., Hatzopoulos, G. N., Agashe, N., Chang, P.-H., Guidotti, N., Reichart, T. M., Reymond, L., Velluz, M., Schneider, F., et al. (2023) · Nature Chemistry · doi:10.1038/s41557-023-01228-8 · Cited by 45 · see citing works
Crystal structure of the tubulin tyrosine carboxypeptidase complex VASH1–SVBP
Adamopoulos, A., Landskron, L., Heidebrecht, T., Tsakou, F., Bleijerveld, O. B., Altelaar, M. A. F., Nieuwenhuis, J., Celie, P. H. N., Brummelkamp, T. R., & Anastassis Perrakis, A. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0254-6 · Cited by 33 · see citing works
Evolutionary Divergence of Enzymatic Mechanisms for Tubulin Detyrosination
van der Laan, S., Lévêque, M. F., Marcellin, G., Vezenkov, L., Lannay, Y., Dubra, G., Bompard, G., Ovejero, S., Urbach, S., Burgess, A., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.11.074 · Cited by 34 · see citing works
Self-citationThe tubulin code in mammalian sperm development and function
Gadadhar, S., Hirschmugl, T., & Janke, C. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.12.003 · Cited by 33 · see citing works
Yue, Y., Hotta, T., Higaki, T., Verhey, K. J., & Ohi, R. (2023) · Current Biology · doi:10.1016/j.cub.2023.07.062 · Cited by 39 · see citing works
Pratt, S. J. P., Lee, R., Chang, K. T., Hernández‐Ochoa, E. O., Annis, D. A., Ory, E. C., Thompson, K. N., Bailey, P. C., Mathias, T. J., Ju, J. A., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009495117 · Cited by 33 · see citing works
Ghasemizadeh, A., Christin, E., Guiraud, A., Couturier, N., Abitbol, M., Risson, V., Girard, E., Jagla, C., Soler, C., Laddada, L., et al. (2021) · eLife · doi:10.7554/elife.70490 · Cited by 33 · see citing works
Hernández, J. M., Parato, J., Sharma, A., Soleilhac, J.-M., Qu, X., Tein, E., Sproul, A. A., Andrieux, A., Goldberg, Y., Moutin, M., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.926914 · Cited by 32 · see citing works
Self-citationMicrotubule-Associated Proteins with Regulatory Functions by Day and Pathological Potency at Night
Oláh, J., Lehotzky, A., Szunyogh, S., Szénási, T., Orosz, F., & Ovádi, J. (2020) · Cells · doi:10.3390/cells9020357 · Cited by 30 · see citing works
α-TubK40me3 is required for neuronal polarization and migration by promoting microtubule formation
Xie, X., Wang, S., Li, M., Diao, L., Pan, X., Chen, J., Zou, W., Zhang, X., Feng, W., & Bao, L. (2021) · Nature Communications · doi:10.1038/s41467-021-24376-2 · Cited by 32 · see citing works
Structural basis of tubulin detyrosination by VASH2/SVBP heterodimer
Zhou, C. Y., Yan, L., Zhang, W., & Liu, Z. (2019) · Nature Communications · doi:10.1038/s41467-019-11277-8 · Cited by 32 · see citing works
Hausrat, T. J., Janiesch, P. C., Breiden, P., Lutz, D., Hoffmeister‐Ullerich, S., Hermans‐Borgmeyer, I., Failla, A. V., & Kneussel, M. (2022) · Nature Communications · doi:10.1038/s41467-022-31776-5 · Cited by 31 · see citing works
A family of carboxypeptidases catalyzing α- and β-tubulin tail processing and deglutamylation
Nicot, S., Gillard, G., Impheng, H., Joachimiak, E., Urbach, S., Mochizuki, K., Włoga, D., Juge, F., & Rogowski, K. (2023) · Science Advances · doi:10.1126/sciadv.adi7838 · Cited by 32 · see citing works
Self-citationThe Tubulin Code and Tubulin-Modifying Enzymes in Autophagy and Cancer
Trisciuoglio, D., & Degrassi, F. (2021) · Cancers · doi:10.3390/cancers14010006 · Cited by 30 · see citing works
Microtubule remodelling as a driving force of axon guidance and pruning
Atkins, M., Nicol, X., & Fassier, C. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.05.030 · Cited by 30 · see citing works
Endogenous Antiangiogenic Factors in Chronic Kidney Disease: Potential Biomarkers of Progression
Tanabe, K., Sato, Y., & Wada, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19071859 · Cited by 29 · see citing works
Fassett, J. T., Xu, X. Y., Kwak, D., Zhu, G., Fassett, E. K., Zhang, P., Wang, H., Mayer, B., Bache, R. J., & Chen, Y. (2019) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2019.03.015 · Cited by 28 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationThe emerging role of tubulin posttranslational modifications in cilia and ciliopathies
He, K., Ling, K., & Hu, J. (2020) · Biophysics Reports · doi:10.1007/s41048-020-00111-0 · Cited by 25 · see citing works
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 25 · see citing works
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 24 · see citing works
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 · see citing works
Microtubule‐associated proteins and enzymes modifying tubulin
Peng, N., & Nakamura, F. (2023) · Cytoskeleton · doi:10.1002/cm.21748 · Cited by 22 · see citing works
CSAP Acts as a Regulator of TTLL-Mediated Microtubule Glutamylation
Bompard, G., van Dijk, J., Cau, J., Lannay, Y., Marcellin, G., Lawera, A., van der Laan, S., & Rogowski, K. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.10.095 · Cited by 24 · see citing works
Self-citationMicrotubule 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 23 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
- Authors
- Aillaud, C., Bosc, C., Peris, L., Bosson, A., Heemeryck, P., Van Dijk, J., Le Friec, J., Boulan, B., Vossier, F., Sanman, L. E., Syed, S., Amara, N., Couté, Y., Lafanechère, L., Denarier, E., Delphin, C., Pelletier, L., Humbert, S., Bogyo, M., Andrieux, A., Rogowski, K., & Moutin, M.-J.
- Affiliations
- Inserm (FR)
- Institut de Génétique Humaine (IGH), Université Montpellier, CNRS UMR9002, 34000 Montpellier, France.
- Grenoble Institut des Neurosciences (GIN), Université Grenoble Alpes, F-38000 Grenoble, France.
- Stanford Medicine (US)
- Team Regulation and Pharmacology of the Cytoskeleton, Institute for Advanced Biosciences, INSERM U 1209, CNRS UMR 5309, Université Grenoble Alpes, 38000 Grenoble, France.
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Andrieux, Annie
- Rogowski, Krzysztof
- Moutin, Marie-Jo
- ORCID
- Aillaud, Chrystelle
- Bosc, Christophe
- Peris, Leticia
- Bosson, Anouk
- Heemeryck, Pierre
- Van Dijk, Juliette
- Le Friec, Julien
- Boulan, Benoit
- Vossier, Frédérique
- Sanman, Laura E.
- Syed, Salahuddin
- Amara, Neri
- Couté, Yohann
- Lafanechère, Laurence
- Denarier, Eric
- Delphin, Christian
- Pelletier, Laurent
- Humbert, Sandrine
- Bogyo, Matthew
- Andrieux, Annie
- Rogowski, Krzysztof
- Moutin, Marie-Jo
- Venue
- Science
- Published
- 2017-12-15
- Volume
- 358
- Issue
- 6369
- Pages
- 1448-1453
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2769672674
- Cited by
- 293
- References
- 37
- Citations by year
- 2026: 24 · 2025: 40 · 2024: 33 · 2023: 31 · 2022: 38 · 2021: 35 · 2020: 40 · 2019: 33 · 2018: 16 · 2017: 3
- FWCI
- 13.72
- Type
- journal article
- Language
- en
- Open access
- green
- hal.science
- Licence
- other-oa
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- HAL (submittedVersion, other-oa)
- Funders
- National Institutes of Health (EB005011)
- Association pour la Recherche sur le Cancer (SFI20111204053, DOC20120605000, 20151203348)
- Agence Nationale de la Recherche (ANR-10-INBS-08-01, ANR-13-JSV2-0002/TYRTUB)
- Institut national de la santé et de la recherche médicale
- Centre National de la Recherche Scientifique
- Commissariat à l"Énergie Atomique et aux Énergies Alternatives
- Université Grenoble Alpes
- La Ligue contre le Cancer, comités Isère et Savoie
- Fondation pour la Recherche Médicale (FDT20160435356)
- Institut National Du Cancer (2016-165)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Keywords
- vasohibin-1, vasohibin-2, microtubule dynamics, neuronal differentiation, neuronal migration, neocortex development, chemoproteomics, irreversible enzyme inhibitors
- MeSH terms
- Animals, Carboxypeptidases, Carrier Proteins, Cell Movement, Female, Humans, Male, Neurons, Tubulin, Tyrosine, Cell Cycle Proteins, Neocortex, Proteomics, Angiogenic Proteins, Mice, Neurogenesis, Gene Knockdown Techniques, HEK293 Cells
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 ›
Are you an author, or do you see a problem with this page? Request a review