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Tau protein function in living cells.
Abstract
Tau protein from mammalian brain promotes microtubule polymerization in vitro and is induced during nerve cell differentiation. However, the effects of tau or any other microtubule-associated protein on tubulin assembly within cells are presently unknown. We have tested tau protein activity in vivo by microinjection into a cell type that has no endogenous tau protein. Immunofluorescence shows that tau protein microinjected into fibroblast cells associates specifically with microtubules. The injected tau protein increases tubulin polymerization and stabilizes microtubules against depolymerization. This increased polymerization does not, however, cause major changes in cell morphology or microtubule arrangement. Thus, tau protein acts in vivo primarily to induce tubulin assembly and stabilize microtubules, activities that may be necessary, but not sufficient, for neuronal morphogenesis.
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“The protein Tau aggregates into tangles in the brain of patients with Alzheimer’s disease.”
From Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau (2017) · cites this paper as [2]
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Cites
Dynamic instability of microtubule growth
Mitchison, T., & Kirschner, M. (1984) · Nature · doi:10.1038/312237a0 · Cited by 3,337
Self-citationCleveland, D. W., Hwo, S.-Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90213-3 · Cited by 915 · cited 2×
“These include the tau proteins of 50-70 kD (Weingarten et al., 1975; Cleveland et al., 1977), microtubule-associated protein 1 (MAP1) ~ of '~330 kD, and microtubule-associated protein 2 (MAP2) of "~300 kD (for a review of MAP1 and MAP2 see Vallee et al., 1984).”
Self-citationPhosphorylation of microtubule-associated proteins regulates their interaction with actin filaments.
Selden, S. C., & Pollard, T. D. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32333-0 · Cited by 314
Cited by
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4051 · Cited by 1,134
Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., & Lee, V. M. Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90057-x · Cited by 903
Stamer, K., Vogel, R., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108057 · Cited by 885
Tau and neurodegenerative disease: the story so far
Iqbal, K., Liu, F., & Gong, C.-X. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.225 · Cited by 806
Ambadipudi, S., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-00480-0 · Cited by 782
Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779
Domains of tau Protein and Interactions with Microtubules
Gustke, N., Trinczek, B., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1994) · Biochemistry · doi:10.1021/bi00198a017 · Cited by 655
Structural Polymorphism of 441-Residue Tau at Single Residue Resolution
Mukrasch, M. D., Bibow, S., Korukottu, J., Jeganathan, S., Biernat, J., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000034 · Cited by 652
Tau stabilizes microtubules by binding at the interface between tubulin heterodimers
Kadavath, H., Hofele, R. V., Biernat, J., Kumar, S., Tepper, K., Urlaub, H., Mandelkow, E., & Zweckstetter, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504081112 · Cited by 524
The microtubule binding domain of tau protein
Lee, G., Neve, R. L., & Kosik, K. S. (1989) · Neuron · doi:10.1016/0896-6273(89)90050-0 · Cited by 500
Proteasome inhibition by paired helical filament‐tau in brains of patients with Alzheimer's disease
Keck, S., Nitsch, R., Grune, T., & Ullrich, O. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01642.x · Cited by 483
Phosphorylation determines two distinct species of tau in the central nervous system
Papasozomenos, S. C., & Binder, L. I. (1987) · Cell Motility · doi:10.1002/cm.970080303 · Cited by 420
LoPresti, P., Szuchet, S., Papasozomenos, S. C., Zinkowski, R. P., & Binder, L. I. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.22.10369 · Cited by 388
The Microtubule-associated Protein Tau Is Extensively Modified with O-linked N-acetylglucosamine
Arnold, C. S., Johnson, G. W., Cole, R. N., Dong, D. L.-Y., Lee, M., & Hart, G. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.28741 · Cited by 361
Wang, J.-Z., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0896-871 · Cited by 360
(1997) · Europe PMC (PubMed Central) · Cited by 354
Analysis of microtubule-associated protein tau glycation in paired helical filaments.
Ledesma, M. D., Bonay, P., Colaço, C., & Avila, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31849-5 · Cited by 333
GSK3: a possible link between beta amyloid peptide and tau protein
Hernández, F., Gómez de Barreda, E., Fuster-Matanzo, A., Lucas, J. J., & Avila, J. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2009.09.011 · Cited by 327
Tau-based therapies in neurodegeneration: opportunities and challenges
Li, C., & Götz, J. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.155 · Cited by 272
Tau Is Enriched on Dynamic Microtubules in the Distal Region of Growing Axons
Black, M. M., Slaughter, T., Moshiach, S., Obrocka, M., & Fischer, I. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-11-03601.1996 · Cited by 270
Glycogen Synthase Kinase 3β Phosphorylates Tau at Both Primed and Unprimed Sites
Cho, J.-H., & Johnson, G. V. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206236200 · Cited by 266
Tau: Enabler of diverse brain disorders and target of rapidly evolving therapeutic strategies
Chang, C.-W., Shao, E., & Mucke, L. (2021) · Science · doi:10.1126/science.abb8255 · Cited by 263
Structural Principles of Tau and the Paired Helical Filaments of Alzheimer's Disease
Mandelkow, E., Von Bergen, M., Biernat, J., & Mandelkow, E. (2007) · Brain Pathology · doi:10.1111/j.1750-3639.2007.00053.x · Cited by 243
The role of pathological tau in synaptic dysfunction in Alzheimer’s diseases
Wu, M., Zhang, M., Yin, X., Chen, K., Hu, Z., Zhou, Q., Cao, X., Chen, Z., & Liu, D. (2021) · Translational Neurodegeneration · doi:10.1186/s40035-021-00270-1 · Cited by 241
Tau Cleavage and Dephosphorylation in Cerebellar Granule Neurons Undergoing Apoptosis
Canu, N., Dus, L., Barbato, C., Ciotti, M. T., Brancolini, C., Rinaldi, A. M., Novak, M., Cattaneo, A., Bradbury, A., & Calissano, P. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-18-07061.1998 · Cited by 232
Tau Does Not Stabilize Axonal Microtubules but Rather Enables Them to Have Long Labile Domains
Qiang, L., Sun, X., Austin, T. O., Muralidharan, H., Jean, D. C., Liu, M., Yu, W., & Baas, P. W. (2018) · Current Biology · doi:10.1016/j.cub.2018.05.045 · Cited by 222
Sun, L., Liu, S. Y., Zhou, X. W., Wang, X. C., Liu, R., Wang, Q., & Wang, J. Z. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00697-8 · Cited by 168
Gao, C., Hölscher, C., Liu, Y., & Li, L. (2012) · revneuro · doi:10.1515/rns.2011.061 · Cited by 164
Sohn, P. D., Tracy, T. E., Son, H.-I., Zhou, Y., Leite, R. E. P., Miller, B. L., Seeley, W. W., Grinberg, L. T., & Gan, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0109-0 · Cited by 160
An Overview on the Clinical Development of Tau-Based Therapeutics
Medina, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19041160 · Cited by 156
Folding of the Tau Protein on Microtubules
Kadavath, H., Jaremko, M., Jaremko, Ł., Biernat, J., Mandelkow, E., & Zweckstetter, M. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201501714 · Cited by 153
Microtubule dynamics in axons and dendrites
Baas, P. W., Slaughter, T., Brown, A., & Black, M. M. (1991) · Journal of Neuroscience Research · doi:10.1002/jnr.490300115 · Cited by 150
Biernat, J., & Mandelkow, E.-M. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.3.727 · Cited by 149
Axonal transport, tau protein, and neurodegeneration in Alzheimer's disease
Terwel, D., Dewachter, I., & Van Leuven, F. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:2:2:151 · Cited by 146
Funk, K. E., Thomas, S. N., Schafer, K. N., Cooper, G. L., Liao, Z., Clark, D. J., Yang, A. J., & Kuret, J. (2014) · Biochemical Journal · doi:10.1042/bj20140372 · Cited by 142
Avila, J., Jiménez, J. S., Sayas, C. L., Bolós, M., Zabala, J. C., Rivas, G., & Hernández, F. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00262 · Cited by 140
Pan, Y., & Nicolazzo, J. A. (2018) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2018.04.009 · Cited by 131
Control of neuronal branching by the death receptor CD95 (Fas/Apo-1)
Zuliani, C., Kleber, S., Klussmann, S., Wenger, T., Kenzelmann, M., Schreglmann, N., Martinez, A., del Rio, J. A., Soriano, E., Vodrazka, P., et al. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401720 · Cited by 117
Propagation of Tau via Extracellular Vesicles
Pérez, M., Avila, J., & Hernández, F. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00698 · Cited by 118
Extracellular Monomeric Tau Is Internalized by Astrocytes
Perea, J. R., López, E., Díez-Ballesteros, J. C., Ávila, J., Hernández, F., & Bolós, M. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00442 · Cited by 114
The Proteasome and Oxidative Stress in Alzheimer's Disease
Bonet-Costa, V., Pomatto, L. C.-D., & Davies, K. J. A. (2016) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6802 · Cited by 99
Hypothesis: microtubules, a key to Alzheimer disease
Matsuyama, S. S., & Jarvik, L. F. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.20.8152 · Cited by 95
Soliman, H. M., Ghonaim, G. A., Gharib, S. M., Chopra, H., Farag, A. K., Hassanin, M. H., Nagah, A., Emad-Eldin, M., Hashem, N. E., Yahya, G., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910794 · Cited by 81
Role of the Lipid Membrane and Membrane Proteins in Tau Pathology
Bok, E., Leem, E., Lee, B.-R., Lee, J. M., Yoo, C. J., Lee, E. M., & Kim, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.653815 · Cited by 61
Yang, J., Zhi, W., & Wang, L. (2024) · Molecules · doi:10.3390/molecules29122812 · Cited by 63
“Tau, a protein that has long been considered to be associated with the axon, binds to axonal microtubules and participates in the stabilisation of microtubules and axonal transport [8].”
BackgroundWada, Y., Ishiguro, K., Itoh, T. J., Uchida, T., Hotani, H., Saito, T., Kishimoto, T., & Hisanaga, S.-I. (1998) · Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022174 · Cited by 58
Perea, J. R., Ávila, J., & Bolós, M. (2018) · Experimental Neurology · doi:10.1016/j.expneurol.2018.08.007 · Cited by 54
Pseudohyperphosphorylation Has Differential Effects on Polymerization and Function of Tau Isoforms
Combs, B., Voss, K., & Gamblin, T. C. (2011) · Biochemistry · doi:10.1021/bi2010569 · Cited by 41
Further understanding of tau phosphorylation: implications for therapy
Medina, M., & Avila, J. (2015) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.2015.1000864 · Cited by 41
Neuronal degeneration, synaptic defects, and behavioral abnormalities in tau45-230 transgenic mice
Lang, A. E., Riherd Methner, D. N., & Ferreira, A. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.06.017 · Cited by 35
Tau; One Protein, So Many Diseases
Tabeshmehr, P., & Eftekharpour, E. (2023) · Biology · doi:10.3390/biology12020244 · Cited by 33
Along the way to a neurofibrillary tangle: a look at the structure of tau
Kosik, K. S., Kowall, N. W., & McKee, A. (1989) · Annals of Medicine · doi:10.3109/07853898909149195 · Cited by 31
Retromer dysfunction at the nexus of tauopathies
Carosi, J. M., Denton, D., Kumar, S., & Sargeant, T. J. (2021) · Cell Death & Differentiation · doi:10.1038/s41418-020-00727-2 · Cited by 16
Metadata
- Authors
- Drubin, D. G., & Kirschner, M. W.
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1986-12-01
- Volume
- 103
- Issue
- 6
- Pages
- 2739-2746
- ISSN
- 0021-9525
- 1540-8140
- PMC
- PMC2114585
- Cited by
- 652
- References
- 3
- Language
- en
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