Cited by 915Microtubule 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
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Microtubule Formation in vitro in Solutions Containing Low Calcium Concentrations
Weisenberg, R. C. (1972) · Science · doi:10.1126/science.177.4054.1104 · Cited by 1,216
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
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Sloboda, 1975, 72, 177
Weingarten, 1975, 72, 1858
Witman, 1976, 73, 4070

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“The group includes MAP1, MAP2, MAP4, Tau, and MAP6 (also known as STOP; Cleveland et al., 1977; Herzog and Weber, 1978; Huber and Matus, 1984; Margolis et al., 1986; Job et al., 1987; Chapin and Bulinski, 1994).”
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“Tau takes role as a potent promoter of tubulin construction in vitro [14].”
Background
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Microtubule destabilization by cdc2/H1 histone kinase: Phosphorylation of a “Pro-rich region” in the microtubule-binding domain of MAP-4
Aizawa, H., Kamijo, M., Ohba, Y., Mori, A., Okuhara, K., Kawasaki, H., Murofushi, H., Suzuki, K., & Yasuda, H. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91760-a · Cited by 34
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In situ localization of Tau mRNA in developing rat brain
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Limited chymotryptic digestion of bovine adrenal 190,000-Mr microtubule-associated protein and preparation of a 27,000-Mr fragment which stimulates microtubule assembly.
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Intracellular and extracellular microtubule associated protein tau as a therapeutic target in Alzheimer disease and other tauopathies
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Altered Levels and Isoforms of Tau and Nuclear Membrane Invaginations in Huntington’s Disease
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“, 1992), the C-terminal region binds to microtubules to regulate their polymerization (Cleveland et al., 1977).”
Background
Hyperphosphorylation induces structural modification of tau‐protein
Uversky, V. N., Winter, S., Galzitskaya, O. V., Kittler, L., & Löber, G. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01303-9 · Cited by 33
Cold stable microtubules in brain studied in fractions and slices
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“Tau proteins (45-60 kD), another faroily of phosphoproteins, are enriched in axons (Weingarten et al., 1975; Cleveland et al., 1977; Lindwall et al., 1984; Binder et al., 1985).”
Background
MAP2 (Microtubule-Associated Protein 2)
Vallee, R. B. (1984) · Springer eBooks · doi:10.1007/978-1-4684-4592-3_8 · Cited by 33
Cellular regulation of microtubule organization.
Olmsted, J. B., Cox, J. V., Asnes, C. F., Parysek, L. M., & Lyon, H. D. (1984) · The Journal of Cell Biology · doi:10.1083/jcb.99.1.28s · Cited by 33
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“Tau facilitates assembly and the stabilization of microtubule polymers (Cleveland et al., 1977; Caceres and Kosik, 1990), modulating microtubule dynamics.”
Background
Systemic and network functions of the microtubule-associated protein tau: Implications for tau-based therapies
Bakota, L., Ussif, A. M., Jeserich, G., & Brandt, R. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.03.003 · Cited by 33
“Originally, tau was identified as a factor that becomes enriched during repeated cycles ofMT assembly and disassembly frombrain homogenates classifying it as aMT protein (Cleveland et al., 1977).”
Background
Wnt signalling pathway and tau phosphorylation: A comprehensive study on known connections
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Tau suppresses microtubule-regulated pancreatic insulin secretion
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Role of tau protein on neocortical and hippocampal oscillatory patterns
Cantero, J. L., Moreno‐López, B., Portillo, F., Rubio, A., Hita-Yáñez, E., & Ávila, J. (2010) · Hippocampus · doi:10.1002/hipo.20798 · Cited by 34
“…proteins; brain oscillations; neocortex; hippocampus; hippocampal-neocortical synchronization INTRODUCTION Tau protein is one of the major neuronal microtubule-associated proteins (MAPs) that was discovered 30 years ago (Weingarten et al., 1975; Cleveland et al., 1977; Fellous et al., 1977).”
Background
Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis
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“Disease related IDPs Amyloid b peptide (Ab) Alzheimer’s disease 40 or 42 Unknown 16 22 (60) Intrinsically disordered Tau Alzheimer’s disease Tauopathy 352 441 Interaction with tubulin to stabilize microtubules and promotion tubulin assembly into microtubules (61) 275 80 and 306 11 (62, 63) Intrinsically disordered (31)”
Background
Development of grape polyphenols as multi-targeting strategies for Alzheimer's disease
Gaamouch, F. E., Liu, K., Lin, H., Wu, C., & Wang, J. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105046 · Cited by 31
Recent advances in using Drosophila to model neurodegenerative diseases
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“The major component of the NFT is tau protein, a highly soluble, microtubule-binding protein normally enriched in axons [71].”
Background
Distribution of MAP‐4 in Cells and in Adult and Developing Mouse Tissuesa
Olmsted, J. B., Asnes, C. F., Parysek, L. M., Lyon, H. D., & Kidder, G. M. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb38401.x · Cited by 31
A putative role for cell cycle‐related proteins in microtubule‐based neuroplasticity
Schmetsdorf, S., Arnold, E., Holzer, M., Arendt, T., & Gärtner, U. (2009) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.06661.x · Cited by 30
“Tau is primarily expressed in neurons where it regulates microtubules stability and assembly (Weingarten et al., 1975; Cleveland et al., 1977a,b; Binder et al., 1985).”
Background
Tau phosphorylation in hippocampus results in toxic gain-of-function
Ávila, J., de Barreda, E. G., Engel, T., Lucas, J. J., & Hernández, F. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380977 · Cited by 33
Expression of Three– and Four–Repeat Tau Isoforms in Mouse Liver
Kenner, L., El‐Shabrawi, Y., Hutter, H., Forstner, M., Zatloukal, K., Höefler, G., Preisegger, K., Kurzbauer, R., & Denk, H. (1994) · Hepatology · doi:10.1002/hep.1840200442 · Cited by 32
Competitive ELISA for the measurement of tau protein in Alzheimer's disease
Harrington, C. R., Edwards, P. C., & Wischik, C. M. (1990) · Journal of Immunological Methods · doi:10.1016/0022-1759(90)90388-c · Cited by 30
The role of PI3K/AKT pathway and its therapeutic possibility in Alzheimer's disease
Yu, H.-J., & Koh, S. (2017) · Hanyang Medical Reviews · doi:10.7599/hmr.2017.37.1.18 · Cited by 30
Non-Rodent Genetic Animal Models for Studying Tauopathy: Review of Drosophila, Zebrafish, and C. elegans Models
Giong, H.-K., Subramanian, M., Yu, K., & Lee, J.-S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168465 · Cited by 31
“Tau is one of the first characterized and well‐known factors to maintain the stability of microtubules (MTs) in the central nervous system (CNS) [10,11].”
Background
Reassessment of Neuronal Tau Distribution in Adult Human Brain and Implications for Tau Pathobiology
Paterno, G., Bell, B. M., Gorion, K.-M. M., Prokop, S., & Giasson, B. I. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01394-9 · Cited by 30
“The physiological functions of tau include promoting tubulin polymerization and MT stability, which are mediated through the MT binding repeat domain of tau and the upstream adjacent proline rich domains [12, 17, 40].”
Background
Rb binding protein Che-1 interacts with Tau in cerebellar granule neurons
Barbato, C., Corbi, N., Canu, N., Fanciulli, M., Serafino, A., Ciotti, M. T., Libri, V., Bruno, T., Amadoro, G., Angelis, R. D., et al. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2003.08.002 · Cited by 29
“Tau protein is a component of the neuronal cytoskeleton, and it plays a crucial role in maintaining the microtubule network (Weingarten et al., 1975; Cleveland et al., 1977; Himmler et al., 1989).”
Background
Overexpression of tau protein in COS-1 cells results in the stabilization of centrosome-independent microtubules and extension of cytoplasmic processes
de Garcini, E. M., de la Luna, S., Domínguez, J. E., & Ávila, J. (1994) · Molecular and Cellular Biochemistry · doi:10.1007/bf01457399 · Cited by 29
“This protein promotes microtubule polymerization in vitro (Cleveland et al., 1977) and stabilizes assembled microtubules in vivo (Drubin and Kirschner, 1986; Caceres and Kosik, 1990).”
Background
Phosphorylation-Induced Structural Reorganization in Tau-Paired Helical Filaments
Rani, L., & Mallajosyula, S. S. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00084 · Cited by 28
Regulation of expression, phosphorylation and biological activity of tau during differentiation in SY5Y cells
Haque, N., Tanaka, T., Iqbal, K., & Grundke, I. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01622-4 · Cited by 29
The misfolding mechanism of the key fragment R3 of tau protein: a combined molecular dynamics simulation and Markov state model study
Liu, H., Zhong, H., Xu, Z., Zhang, Q., Shah, S. J. A., Liu, H., & Yao, X. (2020) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp06954b · Cited by 28
The Accumulation of Tau in Postsynaptic Structures: A Common Feature in Multiple Neurodegenerative Diseases?
Teravskis, P. J., Ashe, K. H., & Liao, D. (2020) · The Neuroscientist · doi:10.1177/1073858420916696 · Cited by 31
Phosphorylated full‐length Tau interacts with 14‐3‐3 proteins via two short phosphorylated sequences, each occupying a binding groove of 14‐3‐3 dimer
Neves, J. F., Petrvalská, O., Bosica, F., Cantrelle, F., Merzougui, H., O’Mahony, G., Hanoulle, X., Obšil, T., & Landrieu, I. (2020) · FEBS Journal · doi:10.1111/febs.15574 · Cited by 29
With the Permission of Microtubules: An Updated Overview on Microtubule Function During Axon Pathfinding
Sánchez-Huertas, C., & Herrera, E. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.759404 · Cited by 32
The Sensitivity of Tau Tracers for the Discrimination of Alzheimer’s Disease Patients and Healthy Controls by PET
Mohammadi, Z., Alizadeh, H., Marton, J., & Cumming, P. D. (2023) · Biomolecules · doi:10.3390/biom13020290 · Cited by 28
“The preponderance of tau expression in the central nervous system (CNS) is in neuronal axons, glia, extracellular space [28,29], and dendrites [30].”
Background
Dysregulation of Microtubule Stability Impairs Morphofunctional Connectivity in Primary Neuronal Networks
Verstraelen, P., Detrez, J. R., Verschuuren, M., Kuijlaars, J., Nuydens, R., Timmermans, J., & Vos, W. H. D. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00173 · Cited by 28
“Tau is one of the MT-stabilizing proteins (Weingarten et al., 1975; Cleveland et al., 1977) with a role in axon elongation (Sayas et al., 2015), release of cargo from motor proteins near the synapse (Medina et al., 2016), and long-term depression of synaptic transmission (Regan et al., 2015).”
Background
The co-polymerization of tubulin and tubulin chochicine complex in the absence and presence of associated proteins.
Sternlicht, H., Ringel, I., & Szasz, J. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70538-9 · Cited by 28
Quantitation and characterization of tau factor in porcine tissues
de Garcini, E. M., Diez, J. C., & Ávila, J. (1986) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(86)90039-5 · Cited by 28
Modulation of tubulin-nucleotide interactions by microtubule-associated proteins: polymerization with ribose-modified analogs of guanosine 5'-triphosphate
Hamel, E., del Campo, A. A., Lustbader, J., & Lin, C. M. (1983) · Biochemistry · doi:10.1021/bi00274a044 · Cited by 28
Novel Tubulin and Tau Neuroprotective Fragments Sharing Structural Similarities with the Drug Candidate NAP (Davuentide)
Gozes, I., Iram, T., Maryanovsky, E., Arviv, C., Rozenberg, L., Schirer, Y., Giladi, E., & Furman-Assaf, S. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131664 · Cited by 27
“The microtubule associated protein tau [57, 58] displays six major isoforms in the adult human brain, all of which are derived by alternative splicing from a single gene, on the long arm of chromosome 17 [59–61].”
Copper(II) Coordination Abilities of the Tau Protein's N‐Terminus Peptide Fragments: A Combined Potentiometric, Spectroscopic and Mass Spectrometric Study
Lukács, M., Szunyog, G., Grenács, Á., Lihi, N., Kállay, C., Natale, G. D., Campagna, T., Lanza, V., Tabbı̀, G., Pappalardo, G., et al. (2019) · ChemPlusChem · doi:10.1002/cplu.201900504 · Cited by 27
The Role of Trace Metals in Alzheimer’s Disease
Benedictis, C. A. D., Vilella, A., & Grabrucker, A. M. (2019) · Codon Publications eBooks · doi:10.15586/alzheimersdisease.2019.ch6 · Cited by 31
“The isoforms differ in the inclusion or exclusion of N repeats (0N or 1N or 2N) at the amino-terminal region and for the presence of three (3R) or four (4R) MT-binding domain (MTB) repeats (R) in the carboxyl-terminal part of the molecule (60).”
Background
Oxidized linoleic acid metabolites regulate neuronal morphogenesis in vitro
Souza, F. D. C., Grodzki, A. C., Morgan, R. K., Zhang, Z., Taha, A. Y., & Lein, P. J. (2023) · Neurochemistry International · doi:10.1016/j.neuint.2023.105506 · Cited by 29
“To evaluate the effects of OXLAMs on axonal morphogenesis, axonal length was quantified in DIV 2 neurons immunopositive for tau-1, a cytoskeletal protein localized to the axons of central neurons (Cleveland et al., 1977; Kanaan and Grabinski, 2021) following a 48 h exposure to an OXLAM or vehicle (0.”
Method
Energy metabolism and protein phosphorylation during apoptosis: a phosphorylation study of tau and high-molecular-weight tau in differentiated PC12 cells*
Davis, P. K., & Johnson, G. V. W. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3400051 · Cited by 27
Tubulin in the nervous system
Gozes, I. (1982) · Neurochemistry International · doi:10.1016/0197-0186(82)90003-1 · Cited by 27
On the use of heat stability as a criterion for the identification of microtubule associated proteins (MAPs)
Vallee, R. B. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(85)91850-9 · Cited by 27
Studying tau protein propagation and pathology in the mouse brain using adeno-associated viruses
Wegmann, S., Bennett, R. E., Amaral, A. C. S., & Hyman, B. T. (2017) · Methods in cell biology · doi:10.1016/bs.mcb.2017.06.014 · Cited by 29
Dynamical decoration of stabilized-microtubules by Tau-proteins
Hervy, J., & Bicout, D. (2019) · Scientific Reports · doi:10.1038/s41598-019-48790-1 · Cited by 27
“4 [38–40], ν = 0.”
Role of microbial dysbiosis in the pathogenesis of Alzheimer's disease
Susmitha, G., & Kumar, R. K. (2023) · Neuropharmacology · doi:10.1016/j.neuropharm.2023.109478 · Cited by 27
Pathological and physiological functional cross-talks of α-synuclein and tau in the central nervous system
Jin, M., Wang, S., Gao, X., Zou, Z., Hirotsune, S., & Sun, L. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.382231 · Cited by 27
“Both αSyn and tau are known to promote MT assembly and stability in vitro (Cleveland et al., 1977; Toba et al., 2017).”
Background

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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