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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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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Properties of the depolymerization products of microtubules from mammalian brain
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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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Background
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Iqbal, K., Zaidi, T., Bancher, C., & Grundke, I. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00650-4 · Cited by 150
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Background
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“Tau is normally found in axons, where it stabilizes microtubules (MTs) through an interaction mediated by the three (3-R) or four (4-R) repeated MT binding domains found in Tau isoforms that are generated by differential splicing (7, 8).”
Background
Tau-Based Treatment Strategies in Neurodegenerative Diseases
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“pressed mainly in neurons, where it regulates microtubule assembly and stability.(1,2) The synthesis of tau is”
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“NFTs are formed by insoluble aggregates of aberrantly hyperphosphorylated tau, which functions normally to stabilize the microtubules of the axonal cytoskeleton (22,23).”
Background
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Goldman, J. E., & Yen, S.-H. C. (1986) · Annals of Neurology · doi:10.1002/ana.410190302 · Cited by 139
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“Purification of tau induces assembly of microtubules (Cleveland et al., 1977).”
Background
Intracellular localization of the high molecular weight microtubule accessory protein by indirect immunofluorescence.
Connolly, J. A., Kalnins, V. I., Cleveland, D. W., & Kirschner, M. W. (1978) · The Journal of Cell Biology · doi:10.1083/jcb.76.3.781 · Cited by 133
“(2) and further purified by elution from SDS-containing polyacrylamide gels.”
BackgroundMethodResultSelf-citation
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Wei, Y., Qu, M.-H., Wang, X.-S., Chen, L., Wang, D.-L., Liu, Y., Hua, Q., & He, R.-Q. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002600 · Cited by 129
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Background
Nonsaturable Binding Indicates Clustering of Tau on the Microtubule Surface in a Paired Helical Filament-like Conformation
Ackmann, M., Wiech, H., & Mandelkow�, E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002590200 · Cited by 138
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Identification of three coated vesicle components as alpha- and beta-tubulin linked to a phosphorylated 50,000-dalton polypeptide.
Pfeffer, S. R., Drubin, D. G., & Kelly, R. B. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.97.1.40 · Cited by 129
“60 p,I of PBS containing 1% BSA was added to the pretreated sample; portions were then incubated with (a) 20/~1 of affinity-purified tubulin antibodies (6), (b) 20/LI of nonimmune rabbit serum to detect nonspecific binding, or (c) 1.”
BackgroundMethod
Liquid–liquid phase separation of tau: From molecular biophysics to physiology and disease
Rai, S. K., Savastano, A., Singh, P., Mukhopadhyay, S., & Zweckstetter, M. (2021) · Protein Science · doi:10.1002/pro.4093 · Cited by 129
“Besides, tau is an amphipathic protein in which the charged residues are distributed non-uniformly and cluster in different domains: a negatively charged N-terminal region (1–150 aa), the strongly positively charged proline-rich region (151–243 aa), a mildly positive repeat domain (244–372 aa), and a slightly negative…”
Background
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Cleveland, D. W., Pittenger, M. F., & Feramisco, J. R. (1983) · Nature · doi:10.1038/305738a0 · Cited by 124
Self-citation
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Liccardo, D., Marzano, F., Carraturo, F., Guida, M., Femminella, G. D., Bencivenga, L., Agrimi, J., Addonizio, A., Melino, I., Valletta, A., et al. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00683 · Cited by 148
“Emerging evidences have demonstrated that astrocyte-mediated neuroinflammation is also involved in the pathogenesis of neurodegenerative diseases, including Frontiers in Physiology | www.frontiersin.org 4 July 2020 | Volume 11 | Article 683 AD (Verkhratsky et al., 2010; Colombo and Farina, 2016).”
Background
Molecular cloning of a ubiquitously distributed microtubule-associated protein with Mr 190,000.
Aizawa, H., Emori, Y., Murofushi, H., Kawasaki, H., Sakai, H., & Suzuki, K. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77426-7 · Cited by 122
Grape Derived Polyphenols Attenuate Tau Neuropathology in a Mouse Model of Alzheimer's Disease
Wang, J., Santa‐María, I., Ho, L., Ksiȩżak-Reding, H., Ono, K., Teplow, D. B., & Pasinetti, G. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101074 · Cited by 123
“Microtubule-associated protein tau is a highly soluble phospho-protein that regulates microtubule stability and polymerization [1,2].”
A Common Amino Acid Sequence in 190-kDa Microtubule-associated Protein and Tau for the Promotion of Microtubule Assembly
Aizawa, H., Kawasaki, H., Murofushi, H., Kotani, S., Suzuki, K., & Sakai, H. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83632-8 · Cited by 121
Expression of the Small Heat-Shock Protein αB-Crystallin in Tauopathies with Glial Pathology
Dabir, D. V., Trojanowski, J. Q., Richter‐Landsberg, C., Lee, V. M. ‐., & Forman, M. S. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63106-9 · Cited by 120
“Tau is a lowmolecular weight microtubule-associated protein that is abundant in the central nervous system where it is expressed predominantly in axons.(2) Tau regulates the assembly and stability of microtubules and this microtubule binding function of tau is negatively regulated by phosphorylation.”
Background
The biochemistry of compounds with anti-microtubule activity in plant cells
Morejohn, L. C., & Fosket, D. E. (1991) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(91)90078-z · Cited by 118
Identification and characterization of the Drosophila tau homolog
Heidary, G., & Fortini, M. (2001) · Mechanisms of Development · doi:10.1016/s0925-4773(01)00487-7 · Cited by 120
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
“group of proteins promoting assembly and stabilization of microtubules (MTs).(20,21) An increase in Tau phosphorylation reduces its affinity for MTs, thereby reducing Tau-mediated polymerization and stabilization of MT structures.”
Background
Chronic lithium treatment decreases tau lesions by promoting ubiquitination in a mouse model of tauopathies
Nakashima, H., Ishihara, T., Suguimoto, S. P., Yokota, O., Oshima, E., Kugo, A., Terada, S., Hamamura, T., Trojanowski, J. Q., Lee, V. M. ‐., et al. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1087-4 · Cited by 119
“Most notably, tau binds to and stabilizes microtubules (MTs), in addition to promoting MT polymerization [7, 10, 37].”
Background
Tau Binds to Lipid Membrane Surfaces via Short Amphipathic Helices Located in Its Microtubule-Binding Repeats
Georgieva, E. R., Xiao, S., Borbat, P. P., Freed, J. H., & Eliezer, D. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.07.046 · Cited by 124
Potential Contribution of Exosomes to the Prion-Like Propagation of Lesions in Alzheimer’s Disease
Vingtdeux, V., Sergeant, N., & Buée, L. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00229 · Cited by 116
“Tau proteins are known to act as promoter of tubulin polymerization in vitro, and are involved in axonal transport (Weingarten et al., 1975; Cleveland et al., 1977; Brandt and Lee, 1993).”
Background
Polymerization of tau peptides into fibrillar structures. The effect of FTDP‐17 mutations
Arrasate, M., Pérez, M., Armas-Portela, R., & Ávila, J. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00210-0 · Cited by 118
The Molecular and Cellular Biology of Tau
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“Tau is a microtubule-associated protein of molecular weight (M,) 50,000 to 64,000 Daltons that serves as a potent promotor of tubulin assembly in vitro (11).”
Background
[39] Purification and assay of microtubule-associated proteins (MAPs)
Sloboda, R. D., & Rosenbaum, J. L. (1982) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(82)85041-6 · Cited by 115
Interactions of taxol, microtubule-associated proteins, and guanine nucleotides in tubulin polymerization.
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BAG-1 Associates with Hsc70·Tau Complex and Regulates the Proteasomal Degradation of Tau Protein
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Presence of tau in isolated nuclei from human brain
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Separation of tubulin from microtubule-associated proteins on phosphocellulose. Accompanying alterations in concentrations of buffer components
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Tau and Axonopathy in Neurodegenerative Disorders
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MAP 4: occurrence in mouse tissues.
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“As shown in Fig. 1 B, all three of the polypeptides present in the microtubule fraction (lane 1) were recovered in the supernatant after boiling (lane 3). Thus, like MAP 2 (16), HeLa 210,000-molwt MAP (41), and tau ( 8 ), the proteins of the MAP 4 complex appear to be thermostable.”
BackgroundMethod
Differences in the developmental patterns of three microtubule- associated proteins in the rat cerebellum
Bernhardt, R. R., Huber, G., & Matus, A. I. (1985) · Journal of Neuroscience · doi:10.1523/jneurosci.05-04-00977.1985 · Cited by 112
The calmodulin‐binding protein in microtubules is tau factor
Sobue, K., Fujita, M., Muramoto, Y., & Kakiuchi, S. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)80447-4 · Cited by 112
Tau in the Pathophysiology of Parkinson’s Disease
Pan, L., Meng, L., He, M., & Zhang, Z. (2021) · Journal of Molecular Neuroscience · doi:10.1007/s12031-020-01776-5 · Cited by 110
Low molecular weight microtubule-associated proteins are light chains of microtubule-associated protein 1 (MAP 1).
Vallee, R. B., & Davis, S. E. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.5.1342 · Cited by 111
Tau biology, tauopathy, traumatic brain injury, and diagnostic challenges
Castellani, R. J., & Perry, G. (2019) · Journal of Alzheimer’s Disease · doi:10.3233/jad-180721 · Cited by 110
A68 proteins in Alzheimer's disease are composed of several tau isoforms in a phosphorylated state which affects their electrophoretic mobilities
Brion, J., Hanger, D. P., Couck, A. M., & Anderton, B. H. (1991) · Biochemical Journal · doi:10.1042/bj2790831 · Cited by 109
High-Mr microtubule-associated proteins: properties and functions
Wiche, G. (1989) · Biochemical Journal · doi:10.1042/bj2590001 · Cited by 108
Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
Oroz, J., Chang, B. J., Wysoczanski, P., Lee, C.-T., Pérez-Lara, Á., Chakraborty, P., Hofele, R. V., Baker, J. D., Blair, L. J., Biernat, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06880-0 · Cited by 100
Microtubule-associated proteins: subunits of the cytomatrix.
Vallee, R. B., Bloom, G. S., & Theurkauf, W. E. (1984) · The Journal of Cell Biology · doi:10.1083/jcb.99.1.38s · Cited by 106
Widespread cellular distribution of MAP-1A (microtubule-associated protein 1A) in the mitotic spindle and on interphase microtubules.
Bloom, G. S., Luca, F. C., & Vallee, R. B. (1984) · The Journal of Cell Biology · doi:10.1083/jcb.98.1.331 · Cited by 106
Untangling Tau and Iron: Exploring the Interaction Between Iron and Tau in Neurodegeneration
Rao, S. S., & Adlard, P. A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00276 · Cited by 108
“The structure of tau is subdivided into three domains, all of which are important in facilitating the interaction of tau with microtubules: (i) the projection domain located in the N-terminal region, determines the spacing between microtubules; (ii) the proline rich domain, comprised of up to seven PXXP motifs that ar…”
Background
The Control of Microtubule Assembly in Vivo
Raff, E. C. (1979) · International review of cytology · doi:10.1016/s0074-7696(08)61660-5 · Cited by 105
Prion-like Spreading in Tauopathies
Ayers, J. I., Giasson, B. I., & Borchelt, D. (2017) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.04.003 · Cited by 106
“Tau refers to microtubule (MT) associated proteins (22, 23) expressed from the MAPT gene located on chromosome 17q21-22 (24, 25).”
Background
Axonal degeneration in tauopathies: disease relevance and underlying mechanisms
Kneynsberg, A., Combs, B., Christensen, K., Morfini, G., & Kanaan, N. M. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00572 · Cited by 102
“The initial discovery of tau protein was based on biochemical procedures that revealed its ability to associate with purified microtubules and modulate their dynamic growth behavior in vitro (Weingarten et al., 1975; Cleveland et al., 1977a,b).”
Background
Immunofluorescence localization of HeLa cell microtubule-associated proteins on microtubules in vitro and in vivo.
Bulinski, J. C., & Borisy, G. G. (1980) · The Journal of Cell Biology · doi:10.1083/jcb.87.3.792 · Cited by 102
Identification of Aminothienopyridazine Inhibitors of Tau Assembly by Quantitative High-Throughput Screening
Crowe, A., Huang, W., Ballatore, C., Johnson, R. L., Hogan, A. L., Huang, R., Wichterman, J., McCoy, J. G., Huryn, D. M., Auld, D. S., et al. (2009) · Biochemistry · doi:10.1021/bi9006435 · Cited by 104
“The ATPZs were also tested for their ability to block the fibrillization of Aβ(1-42), an amyloid peptide found within senile plaques in AD brain (55).”
Influential

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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