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
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Identity and polymerization-stimulatory activity of the nontubulin proteins associated with microtubules
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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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“There were no significant differences between Trembler and control in the distribution of these two polypeptides. extracts, tau composition is primarily low-molecular-weight (LMW) tau, consisting of five or six proteins ranging in size from 50 to 70 kDa on SDS gels (Cleveland et al., 1977).”
Background
Microtubule-associated proteins connect microtubules and neurofilaments in vitro
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Three distinct axonal transport rates for tau, tubulin, and other microtubule-associated proteins: evidence for dynamic interactions of tau with microtubules in vivo
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Casein kinase II preferentially phosphorylates human tau isoforms containing an amino-terminal insert. Identification of threonine 39 as the primary phosphate acceptor.
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“Tau is a microtubule-associated protein (MAP) whose main function is to bind and stabilize microtubules [Weingarten et al., 1975; Cleveland et al., 1977b,a].”
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“to help stabilize microtubule polymers involved in intracellular axonal transport.(16,17) The spreading hypothesis of tau in AD proposes that tau undergoes post-translational”
Background
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[11] Purification of brain microtubules and microtubule-associated protein 1 using taxol
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“Tau is a major neuronal MAP involved in the regulation of microtubule bundling and dynamics (Weingarten et al., 1975; Cleveland et al., 1977a,b; Binder et al., 1985; Chen et al., 1992; Drechsel et al., 1992; Brandt and Lee, 1993b; Trinczek et al., 1995).”
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“In the test tube the assembly-promoting and stabilizing activity of tau increases with the increasing molar ratio of tau to tubulin (Cleveland et al., 1977; Bre and Karsenti, 1990; Panda et al., 1995).”
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A functionally specialized α-tubulin is required for oocyte meiosis and cleavage mitoses in Drosophila
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“MAPK and MAPKKK followed PKC as expected from many previous reports suggesting their roles in AD pathology (Supplementary Material, Table S6).”
BackgroundInfluential
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“Physiologically, tau is a highly soluble microtubule-associated protein important for the assembly and stability of microtubules (2, 3).”
Background
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Tau binding to microtubules does not directly affect microtubule‐based vesicle motility
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“These estimated ratios are close to saturating ratios determined in in vitro studies (Amos, 1977; Cleveland et al., 1977).”
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Immunological characterization of microtubule‐associated proteins specific for the immature brain
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“MAPs can substantially alter the ability of the polymer to assemble and to maintain a particular equilibrium state in vitro ( 10- 13 ), and, due to the intrinsic disassembly characteristics of”
Background
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Differences in microtubule binding and self-association abilities of bovine brain tau isoforms.
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Conservation of microtubule associated proteins. Isolation and characterization of tau and the high molecular weight microtubule associated protein from chicken brain and from mouse fibroblasts and comparison to the corresponding mammalian brain proteins.
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Self-citation
Polymerization of Microtubule-associated Protein Tau under Near-physiological Conditions
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“Tau was isolated using protocols similar to those published by others (Sandoval and Weber, 1980; Johnson et al., 1989), exploiting the protein’s stability to heat treatment (Cleveland et al., 1977a) and solubility in perchloric acid (Lindwall and Cole, 1984).”
BackgroundMethod
Tau: A Signaling Hub Protein
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Neumann, M., Tolnay, M., & Mackenzie, I. R. (2009) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399409001136 · Cited by 80
Protein Kinase FA/GSK‐3 Phosphorylates on Ser235‐Pro and Ser404‐Pro that Are Abnormally Phosphorylated in Alzheimer's Disease Brain
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“One of them is tau, a microtubule-associated protein, which can be aggregated into neuroflibrillary tangles in neurodegenerative diseases, such as AD (Cleveland et al., 1977; Montejo de Garcini et al., 1986).”
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“NFTs are aggregates of hyperphosphorylated tau, a protein essential for microtubule assembly (Cleveland et al., 1977; Harada et al., 1994) whose aberrant conformation has been proposed to induce neurotoxicity.”
Background
Protein kinase C phosphorylates tau and induces its functional alterations
Hoshi, M. M., Nishida, E., Miyata, Y., Sakai, H., Miyoshi, T., Ogawara, H., & Akiyama, T. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80670-1 · Cited by 76
Human Tau Isoforms and Proteolysis for Production of Toxic Tau Fragments in Neurodegeneration
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“Tau binds to microtubules (MT) and is essential for MT stabilization, assembly, and function in neuronal morphology and axonal transport (Weingarten et al., 1975; Cleveland et al., 1977; Ballatore et al., 2007).”
Background
Human tau protein forms complex with PrP and some GSS- and fCJD-related PrP mutants possess stronger binding activities with tau in vitro
Wang, X., Dong, C., Zhang, J., Wan, Y.-Z., Li, F., Huang, Y.-X., Han, L., Shan, B., Gao, C., Han, J., et al. (2007) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-007-9664-6 · Cited by 75
“known capable of regulating the microtubule polymer state and promoting microtubule assembly and stability [1–4].”
Background
Reassembly of flagellar B (alpha beta) tubulin into singlet microtubules: consequences for cytoplasmic microtubule structure and assembly
Linck, R. W. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.89.2.323 · Cited by 75
Interactions between Tau and Different Conformations of Tubulin: Implications for Tau Function and Mechanism
Duan, A. R., Jonasson, E. M., Alberico, E. O., Li, C., Scripture, J. P., Miller, R. A., Alber, M., & Goodson, H. V. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.03.018 · Cited by 85
Identification of centrosomal proteins in a human lymphoblastic cell line.
Gosti, F., Marty, M., Bergès, J., Maunoury, R., & Bornens, M. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04533.x · Cited by 74
Tau Induces Ring and Microtubule Formation from αβ-Tubulin Dimers under Nonassembly Conditions
Devred, F., Barbier, P., Douillard, S., Monasterio, O., Andreu, J. M., & Peyrot, V. (2004) · Biochemistry · doi:10.1021/bi0493160 · Cited by 73
“FIGURE 5: Spectrometric study of tau-tubulin interaction at 20 C (A) Far-UV spectra of 10 íM tau (1), 10 íM tubulin (2), and 10 and 10 íM tau-tubulin mixture (3).”
BackgroundMethodResultInfluential
Phosphorylation by Neuronal cdc2-like Protein Kinase Promotes Dimerization of Tau Protein in Vitro
Paudel, H. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28328 · Cited by 73
Ultrastructural and biochemical classification of pathogenic tau, α-synuclein and TDP-43
Tarutani, A., Adachi, T., Akatsu, H., Hashizume, Y., Hasegawa, K., Saito, Y., Robinson, A., Mann, D. M. A., Yoshida, M., Murayama, S., et al. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02426-3 · Cited by 74
“Under physiological conditions, tau functions to stabilize microtubules and promote their polymerization [67, 68, 141].”
Background
Membrane trafficking in neuronal maintenance and degeneration
Wang, D., Chan, C., Cherry, S., & Hiesinger, P. R. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1201-4 · Cited by 74
“Tau is a microtubule-associated protein (MAP) that stabilizes microtubules [111, 112].”
Background
Immunofluorescent localization of cyclic nucleotide-dependent protein kinases on the mitotic apparatus of cultured cells.
Browne, C. L., Lockwood, A. H., Su, J., Beavo, J. A., & Steiner, A. L. (1980) · The Journal of Cell Biology · doi:10.1083/jcb.87.2.336 · Cited by 71
Cytoplasmic microtubule-associated proteins: Phosphorylation at novel sites is correlated with their incorporation into assembled microtubules
Pallas, D. C., & Solomon, F. (1982) · Cell · doi:10.1016/0092-8674(82)90238-0 · Cited by 71
Structural transitions in tau k18 on micelle binding suggest a hierarchy in the efficacy of individual microtubule‐binding repeats in filament nucleation
Barré, P., & Eliezer, D. (2013) · Protein Science · doi:10.1002/pro.2290 · Cited by 72
Purification and characterization of a 190-kD microtubule-associated protein from bovine adrenal cortex.
Murofushi, H., Kotani, S., Aizawa, H., Hisanaga, S., Hirokawa, N., & Sakai, H. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.5.1911 · Cited by 70
“Brain MAPs fall into three categories, namely MAP1, MAP2, and tau (Sloboda et al., 1976; Murphy et al., 1977; Cleveland et al., 1977).”
Background
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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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