Cited by 916Microtubule and mitosis dynamicsAlzheimer's disease research and treatmentsCancer Treatment and Pharmacology

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Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin

Cleveland, Don W., Hwo, Shu-Ying, Kirschner, Marc W.·1977·Journal of Molecular Biology

DOI 10.1016/0022-2836(77)90213-3

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PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
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Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
Cleveland, D. W., Hwo, S. Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90214-5 · Cited by 881
Self-citation
Microtubule-associated proteins and the stimulation of tubulin assembly in vitro
Sloboda, R. D., Dentler, W. L., & Rosenbaum, J. L. (1976) · Biochemistry · doi:10.1021/bi00665a026 · Cited by 444
PURIFICATION OF TUBULIN AND ASSOCIATED HIGH MOLECULAR WEIGHT PROTEINS FROM PORCINE BRAIN AND CHARACTERIZATION OF MICROTUBULE ASSEMBLY IN VITRO*
Borisy, G. G., Marcum, J. M., Olmsted, J. B., Murphy, D. B., & Johnson, K. A. (1975) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1975.tb19196.x · Cited by 424
Nucleated Assembly of Microtubules in Porcine Brain Extracts
Borisy, G. G., & Olmsted, J. B. (1972) · Science · doi:10.1126/science.177.4055.1196 · Cited by 322
Ultrastructural localization of the high molecular weight proteins associated with in vitro-assembled brain microtubules
Dentler, W., Granett, S. E., & Rosenbaum, J. L. (1975) · The Journal of Cell Biology · doi:10.1083/jcb.65.1.237 · Cited by 261
Identity and polymerization-stimulatory activity of the nontubulin proteins associated with microtubules
Murphy, D. B., Vallee, R. B., & Borisy, G. G. (1977) · Biochemistry · doi:10.1021/bi00631a004 · Cited by 186
Properties of the depolymerization products of microtubules from mammalian brain
Weingarten, M., Suter, M. M., Littman, D. R., & Kirschner, M. W. (1974) · Biochemistry · doi:10.1021/bi00724a012 · Cited by 170
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Kirschner, 1974, 71, 1159
Murphy, 1975, 72, 2696
Shelanski, 1973, 70, 765
Sloboda, 1975, 72, 177
Weingarten, 1975, 72, 1858
Witman, 1976, 73, 4070

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“Tau, and its active role in the assembly of tubulin, was identified in the 1970s (Weingarten et al., 1975; Cleveland et al., 1977), but details of Tau–MT interactions still remain unclear.”
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Background
Microtubule‐associated protein tau is required for axonal neurite elaboration by neuroblastoma cells
Shea, T. B., Beermann, M. L., Nixon, R. A., & Fischer, I. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490320308 · Cited by 60
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Microtubule-Stimulated Phosphorylation of tau at Ser202 and Thr205 by cdk5 Decreases Its Microtubule Nucleation Activity
Wada, 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
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In vitro polymerization of microtubules from HeLa cells.
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“The second group of accessory proteins consists of a number of closely related components with molecular weights in the range of 55-62,000 daltons which have been called the tau fraction (6, 7, 33).”
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“axonal growth and axonal transport [13,14].”
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“It performs important functions in modulating the stability of microtubules and promoting tubulin assembly into microtubules (Cleveland et al., 1977; Elie et al., 2015; Janning et al., 2014).”
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“Tau was firstly discovered via co-purification of proteins that associate with microtubule from the brain lysate, by Mark Kirschner and colleagues [25, 26].”
Background
In situ dephosphorylation of tau by protein phosphatase 2A and 2B in fetal rat primary cultured neurons
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Generation and characterization of new monoclonal antibodies targeting the PHF1 and AT8 epitopes on human tau
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“Tau refers to the microtubule-associated protein [10, 47] expressed from the MAPT gene located on chromosome 17q21–22 [1, 39].”
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Malchiodi‐Albedi, F., Petrucci, T. C., Picconi, B., Iosi, F., & Falchi, M. (1997) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19970601)48:5 · Cited by 53
A comparative study of the in vitro polymerization of tubulin in the presence of the microtubule-associated proteins MAP2 and tau.
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“Posttranslational modifications of Lys residues by acetylation also regulates tau aggregation (Cohen et al., 2011).”
Background
Cell cycle-dependent changes in the dynamics of MAP 2 and MAP 4 in cultured cells.
Olmsted, J. B., Stemple, D. L., Saxton, W. M., Neighbors, B., & McIntosh, J. R. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.1.211 · Cited by 51
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“Tau stabilizes microtubules, thereby promoting the polymerization of tubulin into microtubules [29].”
Background
Evolutionarily conserved regulators of tau identify targets for new therapies
Kim, J., de Haro, M., Al-Ramahi, I., Garaicoechea, L. L., Jeong, H.-H., Sonn, J. Y., Tadros, B., Liu, Z., Botas, J., & Zoghbi, H. Y. (2023) · Neuron · doi:10.1016/j.neuron.2022.12.012 · Cited by 50
“There are six isoforms of tau, produced by alternative splicing of microtubule-associated protein tau (MAPT) but all of them stabilize microtubules and therefore play roles in intraneuronal transport.(5,6) Hyperphosphorylation of tau promotes its accumulation notably in AD, where it forms the hallmark neurofibrillary…”
Background
N-terminal Truncation of Microtubule Associated Protein Tau Dysregulates its Cellular Localization
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“Via regulation of microtubule stability and integrity, tau plays important role in maintenance of neuron cell shape, axonal transport, and signal transduction [1, 2].”
Background
Behavioral Abnormalities in Knockout and Humanized Tau Mice
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“Tau is a microtubule-associated protein abundant in the Central Nervous System (CNS) with its most well-characterized biological function being microtubules polymerization (1, 2).”
Background
Differences in the abilities of human tau isoforms to promote microtubule assembly
Scott, C. W., Blowers, D. P., Barth, P. T., Lo, M. M. S., Salama, A. I., & Caputo, C. B. (1991) · Journal of Neuroscience Research · doi:10.1002/jnr.490300116 · Cited by 53
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Dynamic interactions of fluorescently labeled microtubule-associated proteins in living cells.
Scherson, T. Y., Kreis, T. E., Schlessinger, J., Littauer, U. Z., Borisy, G. G., & Geiger, B. (1984) · The Journal of Cell Biology · doi:10.1083/jcb.99.2.425 · Cited by 50
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Competitive inhibition of colchicine binding to tubulin by microtubule-associated proteins.
Nunez, J., Fellous, A., Francon, J., & Lennon, A. M. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.1.86 · Cited by 49
Affinity Purification of Human τ Proteins and the Construction of a Sensitive Sandwich Enzyme‐Linked Immunosorbent Assay for Human τ Detection
Mercken, M. H., Vandermeeren, M., Lübke, U., Six, J., Boons, J., Vanmechelen, E., VOORDE, A. V. D., & Gheuens, J. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb09754.x · Cited by 50
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Assembly of unfertilized sea urchin egg tubulin at physiological temperatures.
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Background
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Kinesin and tau bind to distinct sites on microtubules
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The tau proteins in neuronal growth and development
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“The procedure of cycled assembly yields as major MAPs, several highmolecular weight proteins (MAP1A, MAP1B(MAP5), and MAP2) with molecular weights >200 kDa, and the tau proteins, a family of closely related low molecular weight phosphoproteins with a mass between 50 and 70 kDa (6, 7).”
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“MAPs constitute a complex family of proteins, including MAP2, MAP4, Mip-90, tau and STOP, many of which have been shown to regulate tubulin polymerisation and function [23-25].”
Background
Kinetic and steady-state analysis of microtubules in the presence of colchicine
Deery, W. J., & Weisenberg, R. C. (1981) · Biochemistry · doi:10.1021/bi00511a038 · Cited by 47
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“Under physiological conditions, tau protein forms a complex with tubulin and promotes microtubule assembly (Cleveland et al., 1977 ; Weingarten et al., 1975 ).”
Binding of glyceraldehyde 3-phosphate dehydrogenase to microtubules
Durrieu, C., Bernier-Valentin, F., & Rousset, B. (1987) · Molecular and Cellular Biochemistry · doi:10.1007/bf00221912 · Cited by 46
Expression of Various Microtubule‐Associated Protein 2 Forms in the Developing Mouse Brain and in Cultured Neurons and Astrocytes
Charrière‐Bertrand, C., Garner, C. C., Tardy, M., & Nunez, J. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb08163.x · Cited by 46
Different tubulin polymers are produced by microtubule-associated proteins MAP2 and tau in the presence of guanosine 5'-(alpha, beta-methylene)triphosphate.
Sandoval, I. V., & Weber, K. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70500-6 · Cited by 46
Purification, characterization, and assembly properties of tubulin from unfertilized eggs of the sea urchin Strongylocentrotus purpuratus
Detrich, H. W., & Wilson, L. (1983) · Biochemistry · doi:10.1021/bi00279a023 · Cited by 46
Misfolded tau protein and disease modifying pathways in transgenic rodent models of human tauopathies
Žilka, N., Korenova, M., & Novák, M. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0499-y · Cited by 47
“transport [26, 27].”
Disruption of nuclear envelope integrity as a possible initiating event in tauopathies
Prissette, M., Fury, W., Koss, M., Racioppi, C., Fedorova, D., Dragileva, E., Clarke, G., Pohl, T., Dugan, J., Ahrens, D., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111249 · Cited by 41
Phosphorylation of Tau Alters Its Association with the Plasma Membrane
Ekinci, F. J., & Shea, T. B. (2000) · Cellular and Molecular Neurobiology · doi:10.1023/a:1007075115574 · Cited by 45
“The ability of tau to stabilize microtubules in cell-free analyses and within cells (Bass et al., 1994; Cleveland et al., 1977; Dreschel et al., 1992; Drubin and Kirschner, 1986; Takemura et al., 1992), coupled with its segregation within axons (Binder et 1 Center for Cellular Neurobiology and…”
Background
Purification of microtubule protein from beef brain and comparison of the assembly requirements for neuronal microtubules isolated from beef and hog
Murphy, D. B., & Hiebsch, R. R. (1979) · Analytical Biochemistry · doi:10.1016/0003-2697(79)90577-3 · Cited by 45
PACSIN proteins in vivo: Roles in development and physiology
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The fluorescent pentameric oligothiophene pFTAA identifies filamentous tau in live neurons cultured from adult P301S tau mice
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Authors: Cleveland, D. W., Hwo, S.-Y., & Kirschner, M. W.
Affiliations: Princeton University (US)
ORCID: Cleveland, Don W.
Kirschner, Marc W.
Venue: Journal of Molecular Biology
Publisher: Elsevier BV
Published: 1977-10
Volume: 116
Issue: 2
Pages: 207-225
ISSN: 0022-2836 (ISSN-L)
DOI: 10.1016/0022-2836(77)90213-3
OpenAlex: W1971165215
Cited by: 915
References: 18
Citations by year: 2026: 12 · 2025: 19 · 2024: 20 · 2023: 25 · 2022: 24 · 2021: 43 · 2020: 26 · 2019: 29 · 2018: 26 · 2017: 36 · 2016: 20 · 2015: 20 · 2014: 24 · 2013: 16 · 2012: 20
FWCI: 11.02
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Journal of Molecular Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
Keywords: tau protein, microtubule-associated proteins, tubulin, microtubule assembly, microtubule nucleation, microtubule depolymerization, critical concentration, protein purification, phosphocellulose chromatography, ring structure
MeSH terms: Chromatography, Agarose, Electrophoresis, Polyacrylamide Gel, Glycoproteins, Microtubules, Molecular Weight, Proteins, Tubulin

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Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin

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