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
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Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
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Self-citation
Microtubule-associated proteins and the stimulation of tubulin assembly in vitro
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PURIFICATION OF TUBULIN AND ASSOCIATED HIGH MOLECULAR WEIGHT PROTEINS FROM PORCINE BRAIN AND CHARACTERIZATION OF MICROTUBULE ASSEMBLY IN VITRO*
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Nucleated Assembly of Microtubules in Porcine Brain Extracts
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Ultrastructural localization of the high molecular weight proteins associated with in vitro-assembled brain microtubules
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Identity and polymerization-stimulatory activity of the nontubulin proteins associated with microtubules
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Properties of the depolymerization products of microtubules from mammalian brain
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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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“Under normal physiological conditions, tau interacts with tubulin to support microtubule assembly [30, 31].”
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[Tauopathy and Alzheimer disease: a full degenerating process].
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Molecular diversity at the carboxyl terminus of human and rat tau
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A τ‐Related Protein of 130 kDa Is Present in Alzheimer Brain
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Heterogeneity of the High Molecular Weight τ Proteins in N115 Neuroblastoma Cells
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Colchicine binding to an oligomer of tubulin
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“Tau binds microtubule filaments (Cleveland et al., 1977; Weingarten et al., 1975) through interactions across the interface”
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“Tau protein was initially co-purified with tubulin and subsequently identified as a microtubule-assembly factor (Cleveland et al. 1977; Weingarten et al. 1975; Witman et al. 1976).”
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“Tau protein is a highly soluble phosphoprotein and the most important protein of the axonal cytoskeleton [6, 10].”
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“Because each 7 polypeptide showed almost the same peptide patterns as reported previously (Cleveland et al., 1977b; Garner et al., 1988; data not shown), the second largest 7 polypeptide was used in this experiment.”
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A 26–30 kDa developmentally‐regulated tauisoform localized within nuclei of mitotic humanneuroblastoma cells
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“…is required (Gozes and Littauer, 1978; Gozes and Sweadner, 1981; Gozes and Barnstable, 1982), but most notably, the tubulinassociated unit (tau, Cleveland et al., 1977; Garcia and Cleveland, 2001) and the microtubule-associated proteins (MAP) are important as well (Nunez and Fischer, 1999).”
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Application of Immunofluorescence in Studies of Cytoskeletal Antigens
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“36 Cellular energy in the form of ATP and GTP is also needed for microtubule stability and growth, and in the absence or depletion of bioavail-able energy, microtubules can depolymerize.”
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“We tested DCX (double-cortin) and tau, two MAPs known to stimulate GTP-tubulin assembly (Cleveland et al., 1977; Moores et al., 2006).”
High-yield purification of fetal tau preserving its structure and phosphorylation pattern
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Neuronal cytoplasmic inclusions in tau, TDP-43, and FUS molecular subtypes of frontotemporal lobar degeneration share similar spatial patterns
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“Compared with tau, which is widespread in neurons and important in the assembly and stabilisation of microtubules [27,51], both TDP-43 and FUS have more specific roles, TDP-43 in mRNA function, DNA repair, and in non-coding RNA metabolism [45] while FUS is important in regulating gene expression including transcriptio…”
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Strains of Pathological Protein Aggregates in Neurodegenerative Diseases
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Tubulin from a development insect embryo undergoing rapid mitosis: Factors regulating in vitro assembly of tubulin from Drosophila melanogaster
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Thyroid Hormones
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A pathological phosphorylation pattern enhances tau cooperativity on microtubules and facilitates tau filament assembly
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Neural stem cells derived from the developing forebrain of YAC128 mice exhibit pathological features of Huntington’s disease
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“Tau is an intracellular, soluble protein that is critical for po-lymerizing and stabilizing microtubules in neurons (Cleveland et al. 1977; Iqbal et al. 1986).”
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“In healthy neurons, Tau binds to microtubules to promote their polymerization and stability (Weingarten et al., 1975; Cleveland et al., 1977; Panda et al., 2003).”
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The Role of Aβ and Tau Oligomers in the Pathogenesis of Alzheimer’s Disease
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Tauopathy induces degeneration and impairs regeneration of sensory nerves in the cornea
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Functional Cooperation of α-Synuclein and Tau Is Essential for Proper Corticogenesis
Wang, S., Fu, Y., Miyata, T., Matsumoto, S., Shinoda, T., Itoh, K., Harada, A., Hirotsune, S., & Jin, M. (2022) · Journal of Neuroscience · doi:10.1523/jneurosci.0396-22.2022 · Cited by 8
Constitutive expression of p21H‐Rasval12 in neurons induces increased axonal size and dendritic microtubule density in vivo
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“It might be likely that in transgenic mice, an exaggerated presence of tau protein promotes microtubule polymerization (Cleveland et al., 1977; Hirokawa et al., 1988; Hirokawa, 1995; Al-Bassam et al., 2002).”
Background
Paradoxical phosphorylation of the serine 199 on tau proteins from young individuals
Maurage, C., Sergeant, N., Ruchoux, M., Hauw, J., & Delacourte, A. (2001) · Neuroreport · doi:10.1097/00001756-200110290-00007 · Cited by 8
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Use of CK-548 and CK-869 as Arp2/3 complex inhibitors directly suppresses microtubule assembly both in vitro and in vivo
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Structure and Chemistry of Microtubules
Dustin, P. (1984) · Springer eBooks · doi:10.1007/978-3-642-69652-7_5 · Cited by 8
Données fondamentales sur les pathologies amyloïde et Tau dans la maladie d’Alzheimer : quelles perspectives thérapeutiques ?
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The `assembly‐promoting sequence region' of microtubule‐associated protein 4 failed to promote microtubule assembly
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Increased ALZ-50 immunoreactivity in CSF of pseudotumor cerebri patients.
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Biochemical and immunochemical identification of a microtubule‐binding protein from bovine pancreas
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Purification and characterization of a Mn2+/phospholipid-dependent protein phosphatase from pig brain membranes
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Different assembly properties of cod, bovine, and rat brain microtubules
Fridén, B., Strömberg, E., & Wallin, M. (1992) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970210406 · Cited by 8
Microtubule Proteins and P-Proteins
Sabnis, D. D., & Hart, J. W. (1982) · Springer eBooks · doi:10.1007/978-3-642-68237-7_12 · Cited by 8
Linear and Nonlinear Dielectric Response of Intrinsically Disordered Proteins
Sauer, M. A., Colburn, T., Maiti, S., Heyden, M., & Matyushov, D. V. (2024) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.4c00866 · Cited by 7
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Tang, F., Wei, J., Wong, M.-L., & Lei, P. (2025) · Genomic psychiatry : · doi:10.61373/gp025i.0122 · Cited by 7
Role of proline‐rich tyrosine kinase 2 (Pyk2) in the pathogenesis of Alzheimer's disease
Kumar, R. K., Tiwari, V., & Dey, S. (2021) · European Journal of Neuroscience · doi:10.1111/ejn.15569 · Cited by 9
“Tau protein is the major component of NFTs and forms a complex with tubulin and promotes the stabilization of microtubules assembly (Cleveland et al., 1977; Weingarten et al., 1975).”
Background
Site-Specific C-Terminal Fluorescent Labeling of Tau Protein
Bryan, L. C., Awasthi, S., Li, Y., Nirmalraj, P. N., Balog, S., Yang, J., & Mayer, M. (2022) · ACS Omega · doi:10.1021/acsomega.2c06139 · Cited by 7
“5,6 Human Tau protein exists in six different isoforms ranging in length from 352 to 441 amino acids that vary in the number of N-terminal inserts (N1 and N2) and contain three or four imperfect repeats (R1 − R4).”
Brain microdialysate tau dynamics predict functional and neurocognitive recovery after poor-grade subarachnoid haemorrhage
Heilig, M., Rass, V., Lindner, A., Kofler, M., Ianosi, B., Gaasch, M., Putnina, L., Humpel, C., Scherfler, C., Zamarian, L., et al. (2022) · Brain Communications · doi:10.1093/braincomms/fcac342 · Cited by 7
Tau pathology: predictive diagnostics, targeted preventive and personalized medicine and application of advanced research in medical practice
Gozes, I. (2010) · The EPMA Journal · doi:10.1007/s13167-010-0029-y · Cited by 7
“MAPs binding to tubulin/microtubules enables them to play a fundamental role in promoting microtubule assembly and stability [6, 9, 10].”
Background
Molecular dynamics simulations reveal the disruption mechanism of a 2,4‐thiazolidinedione derivative C30 against tau hexapeptide ( PHF6 ) oligomer
Liu, H., Zhong, H., Liu, H., & Yao, X. (2021) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26196 · Cited by 7
“Normally, it binds to microtubules, promoting microtubule stabilization, and facilitating axonal transport.(11,12) In the regulation of specific kinases and phosphatases, tau is in a dynamic equilibrium between microtubule-bound and microtubule-unbound”
Background
Investigating Pathogenetic Mechanisms of Alzheimer’s Disease by Systems Biology Approaches for Drug Discovery
Yeh, S., Chung, M.-H., & Chen, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011280 · Cited by 7
“Tau proteins interact with tubulin to facilitate tubulin formation into microtubules and maintain the stability of microtubules [52].”
Background
History of Dementia
Boller, F. (2008) · Handbook of clinical neurology · doi:10.1016/s0072-9752(07)01201-8 · Cited by 8
“Tau (which is the abbreviation of “tubulin associated unit”), a microtubule-associated protein isolated in 1977, greatly facilitates the polymerization of neurotubules (Cleveland et al., 1977) and is the main constituent of NFTs (Grundke-Iqbal et al.”
Background
Alternative Splicing of Amino-Terminal Tau mRNA in Rat Spinal Cord during Development and Following Axonal Injury
Halverson, R. A., Chambers, C. B., & Muma, N. A. (2001) · Experimental Neurology · doi:10.1006/exnr.2001.7637 · Cited by 7
Tau Microheterogeneity: An Immunological Approach with Monoclonal Antibodiesa
Fellous, A., Ohayon, R., Mazié, J. C., Rosa, F., Ludueña, R. F., & Prasad, V. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb38397.x · Cited by 7
Purification and characterization of a new, ubiquitously distributed class of microtubule‐associated protein with molecular mass 250 kDa
Katsuki, M., Tokuraku, K., Nakagawa, H., & Kotani, S. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01822.x · Cited by 7
Pathways to Amyloid Fibril Formation: Partially Folded Intermediates in the Fibrillation of Natively Unfolded Proteins
Uversky, V. N., & Fink, A. L. (2005) · Wiley eBooks · doi:10.1002/9783527619344.ch11 · Cited by 7
A 70 kD microtubule‐binding protein from starfish eggs: Purification, characterization, and localization during meiosis and mitosis
Hosoya, N., Hosoya, H., Mohri, T., & Mohri, H. (1990) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970150306 · Cited by 7
Tau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axonsPreprint
Hahn, I., Voelzmann, A., Parkin, J., Fülle, J. B., Slater, P. G., Lowery, L. A., Sánchez‐Soriano, N., & Prokop, A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.19.257808 · Cited by 6
Travels with tau prions
Diamond, M. I. (2023) · Cytoskeleton · doi:10.1002/cm.21806 · Cited by 5
“Tau was separately identified and purified by the Kirschner lab as a microtubule-associated protein (Cleveland et al., 1977; Weingarten et al., 1975).”
Method
Severe neurodegeneration in brains of transgenic rats producing human tau prions
Ayers, J. I., Lopez, T. P., Steele, I. T., Oehler, A., Roman-Albarran, R., Cleveland, E., Chong, A., Carlson, G. A., Condello, C., & Prusiner, S. B. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02771-5 · Cited by 7
“Tau is encoded by the MAPT gene and is highly expressed in neurons where it promotes axonal microtubule assembly [19, 51, 77].”
La protéine microtubulaire Tau testiculaire : une place dans la spermatogenèse ?
Sigala, J., Jumeau, F., Buée, L., Sergeant, N., & Mitchell, V. A. (2015) · Morphologie · doi:10.1016/j.morpho.2015.03.001 · Cited by 8

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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