Cited by 929Alzheimer's disease research and treatmentsMicrotubule and mitosis dynamicsNeuroinflammation and Neurodegeneration Mechanisms

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Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.

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Goedert, M., Jakes, R.·1990·The EMBO Journal

DOI 10.1002/j.1460-2075.1990.tb07870.xPMC PMC552204

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Abstract

We have expressed six previously cloned isoforms of human microtubule-associated tau protein in Escherichia coli and purified them to homogeneity in a biologically active form. They range from 352 to 441 amino acids in length and differ from each other by the presence of three or four tandem repeats in the carboxy-terminal half and by the presence or absence of 29 or 58 amino acid inserts in the amino-terminus. When mixed together they gave a set of six bands on SDS-PAGE gels with apparent molecular weights of 48-67 kd and with a characteristic pattern of spacings. Four of these bands aligned with the major tau bands found in adult human cerebral cortex following perchloric acid extraction and alkaline phosphatase treatment. They consisted of isoforms with three repeats and no insertions, four repeats and no amino-terminal insertions and three- and four-repeat containing isoforms with the 29 amino acid insertion. In fetal human brain extracts treated with alkaline phosphatase one of the two major tau bands aligned with the three-repeat containing isoform with no insertions, whereas the molecular nature of the second major tau band remains to be established. The recombinant tau isoforms were biologically active at micromolar concentrations, as assessed by their ability to promote microtubule assembly. The rates of assembly were 2.5-3.0 times faster for isoforms containing four repeats when compared with three-repeat containing isoforms, with no significant contribution by the amino-terminal insertions.

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Molecular aging of tau: disulfide‐independent aggregation and non‐enzymatic degradation in vitro and in vivo
Watanabe, A., Hong, W., Dohmae, N., Takio, K., Morishima‐Kawashima, M., & Ihara, Y. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02611.x · Cited by 51
“The pellets were re-suspended in the extraction buffer [50 mM PIPES, 1 mM EGTA, 1 mM dithiothreitol (DTT), 0.5 mM phenylmethyulsulfonyl fluoride (PMSF), 0.5 lg/mL leupeptin, pH 6.8], as described previously (Goedert and Jakes 1990; Hasegawa et al. 1998).”
MethodInfluential
Meta-analysis of the association between variants in MAPT and neurodegenerative diseases
Zhang, C., Zhu, J., Wan, Y., Tan, L., Wang, H.-F., Yu, J., & Tan, L. (2017) · Oncotarget · doi:10.18632/oncotarget.16690 · Cited by 57
“3, and encodes six tau isoforms ranging from 352 to 441 amino acids in length expressed in neurons [18].”
Background
Soluble Tau has devastating effects on the structural plasticity of hippocampal granule neurons
Bolós, M., Pallas‐Bazarra, N., Terreros‐Roncal, J., Perea, J. R., Jurado‐Arjona, J., Ávila, J., & Llorens-Martín, M. (2017) · Translational Psychiatry · doi:10.1038/s41398-017-0013-6 · Cited by 55
“During the human lifespan, Tau protein expression and function are intricately regulated by alternative splicing and post-transcriptional modi ﬁ cations 7 – 9 .”
Ultrastructural instability of paired helical filaments from corticobasal degeneration as examined by scanning transmission electron microscopy.
Ksiȩżak-Reding, H., Tracz, E., Yang, L., Dickson, D. W., Simon, M. N., & Wall, J. S. (1996) · Europe PMC (PubMed Central) · Cited by 51
The genetics of frontotemporal lobar degeneration
Rademakers, R., & Hutton, M. (2007) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-007-0067-6 · Cited by 51
Single Posttranslational Modifications in the Central Repeat Domains of Tau4 Impact its Aggregation and Tubulin Binding
Ellmer, D., Brehs, M., Haj‐Yahya, M., Lashuel, H. A., & Becker, C. F. W. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201805238 · Cited by 49
Four-Repeat Tauopathies: Current Management and Future Treatments
VandeVrede, L. A., Ljubenkov, P. A., Rojas, J. C., Welch, A. E., & Boxer, A. L. (2020) · Neurotherapeutics · doi:10.1007/s13311-020-00888-5 · Cited by 55
Quinones Facilitate the Self-Assembly of the Phosphorylated Tubulin Binding Region of Tau into Fibrillar Polymers
Santa‐María, I., Hernández, F., Martín, C. P., Ávila, J., & Moreno, F. J. (2004) · Biochemistry · doi:10.1021/bi035345j · Cited by 51
Characterization of tau proteins in human neuroblastoma SH-SY5Y cell line
Uberti, D. L., Rizzini, C., Spano, P., & Memo, M. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00715-5 · Cited by 51
Phosphorylation, calpain proteolysis and tubulin binding of recombinant human tau isoforms
Litersky, J. M., Scott, C. W., & Johnson, G. V. W. (1993) · Brain Research · doi:10.1016/0006-8993(93)90349-r · Cited by 51
Tau and Alpha Synuclein Synergistic Effect in Neurodegenerative Diseases: When the Periphery Is the Core
Vacchi, E., Kaelin‐Lang, A., & Melli, G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21145030 · Cited by 51
“In the adult brain, 0N and 1N isoforms represent 37 to 54% of total tau, while 2N isoforms are only 9% [12].”
Background
Molecular Cloning and Functional Characterization of Chicken Brain Tau: Isoforms with up to Five Tandem Repeats
Yoshida, H., & Goedert, M. (2002) · Biochemistry · doi:10.1021/bi026464m · Cited by 50
Self-citation
Progressive supranuclear palsy: A systematic review
Rampello, L., Buttà, Raffaele, R., Vecchio, I., Battaglia, G., Cormaci, G. F., & Alvano, A. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.03.013 · Cited by 50
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
Differential Distribution of Tau Proteins in Developing Cat Cerebral Cortex and Corpus Callosum
Riederer, B. M., & Innocenti, G. M. (1991) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1991.tb00048.x · Cited by 50
“fact the juvenile taus are less effective in the polymerization of microtubules may be due to a lack of sequences encoded by exons 2, 3 and 10 (Goedert and Jakes, 1990), although phosphorylation can also influence the function of juvenile taus (see discussion below).”
Background
The natural osmolyte trimethylamine N‐oxide (TMAO) restores the ability of mutant tau to promote microtubule assembly
Smith, M. J., Crowther, R. A., & Goedert, M. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02169-4 · Cited by 49
Self-citation
Isoform-independent and -dependent phosphorylation of microtubule-associated protein tau in mouse brain during postnatal development
Tuerde, D., Kimura, T., Miyasaka, T., Furusawa, K., Shimozawa, A., Hasegawa, M., Ando, K., & Hisanaga, S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.798918 · Cited by 47
Tau Pathology is PresentIn Vivoand DevelopsIn Vitroin Sensory Neurons from Human P301S Tau Transgenic Mice: A System for Screening Drugs against Tauopathies
Mellone, M., Kestoras, D., Andrews, M. R., Dassie, E., Crowther, R. A., Stokin, G. B., Tinsley, J. M., Horne, G., Goedert, M., Tolkovsky, A. M., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.4933-12.2013 · Cited by 44
“Soluble tau was extracted essentially as previously described (Goedert and Jakes, 1990).”
MethodSelf-citation
The influence of dynein processivity control, MAPs, and microtubule ends on directional movement of a localising mRNA
Soundararajan, H. C., & Bullock, S. L. (2014) · eLife · doi:10.7554/elife.01596 · Cited by 48
“Human tau23 (352 AA, 0 inserts and 3 repeats–0N3R, shortest isoform) was expressed in bacteria (BL21(DE3) strain), purified, and fluorescently labelled with Alexa-488 maleimide as previously described (Goedert and Jakes, 1990; McVicker et al., 2011).”
Method
PSF Suppresses Tau Exon 10 Inclusion by Interacting with a Stem-Loop Structure Downstream of Exon 10
Ray, P., Kar, A. N., Fushimi, K., Havlioglu, N., Chen, X., & Wu, J. Y. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9634-z · Cited by 51
“Tau4R and Tau3R isoforms differ in their binding affinity to microtubules (Lee et al. 1989; Goedert and Jakes 1990; Goode et al. 2000; Utton et al. 2002; Tomoo et al. 2005; Konzack et al. 2007; LeBoeuf et al. 2008).”
Background
An extensive network of PHFτ‐rich dystrophic neurites permeates neocortex and nearly all neuritic and diffuse amyloid plaques in Alzheimer disease
Schmidt, M. L., Didario, A. G., Lee, V. M. ‐., & Trojanowski, J. Q. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00259-2 · Cited by 47
The tau proteins in neuronal growth and development
Brandt, R. (1996) · Frontiers in bioscience · doi:10.2741/a120 · Cited by 47
Glycogen synthase kinase 3 phosphorylates recombinant human tau protein at serine‐262 in the presence of heparin (or tubulin)
Moreno, F. J., Medina, M., Pérez, M., de Garcini, E. M., & Ávila, J. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00934-2 · Cited by 47
Acetylation discriminates disease-specific tau deposition
Chakraborty, P., Rivière, G., Hebestreit, A., de Opakua, A. I., Vorberg, I. M., Andreas, L. B., & Zweckstetter, M. (2023) · Nature Communications · doi:10.1038/s41467-023-41672-1 · Cited by 52
“3R and 4R tau isoforms differ in their ability to regulate microtubule dynamics 7 .”
Background
Brain-penetrant microtubule-stabilizing compounds as potential therapeutic agents for tauopathies
Brunden, K. R., Ballatore, C., Lee, V. M. ‐., Smith, A. B., & Trojanowski, J. Q. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120010 · Cited by 46
Tau/MAPT disease-associated variant A152T alters tau function and toxicity via impaired retrograde axonal transport
Butler, V. J., Salazar, D. A., Soriano‐Castell, D., Alves‐Ferreira, M., Dennissen, F. J. A., Vohra, M., Osés-Prieto, J. A., Li, K. H., Wang, A. L., Jing, B., et al. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy442 · Cited by 44
“The 1N4R tau isoform is the most abundant adult human brain isoform (25,26).”
Background
Tubulin assembly is disordered in a hypogeomagnetic field
Wang, D. L., Wang, X. S., Xiao, R., Liu, Y. M., & He, R. Q. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.08.156 · Cited by 46
“Recombinant tau23 protein was expressed and purified as described previously [18,27,28] (panel a).”
Method
Using Intramolecular Disulfide Bonds in Tau Protein to Deduce Structural Features of Aggregation-resistant Conformations
Walker, S., Ullman, O., & Stultz, C. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.336107 · Cited by 46
The FK506-binding protein FKBP52in vitroinduces aggregation of truncated Tau forms with prion-like behavior
Giustiniani, J., Guillemeau, K., Dounane, O., Sardin, E., Huvent, I., Schmitt, A., Hamdane, M., Buée, L., Landrieu, I., Lippens, G. M., et al. (2015) · The FASEB Journal · doi:10.1096/fj.14-268243 · Cited by 48
“Recombinant, wild-type, full-length Tau protein was expressed in Escherichia coli from clone hT40 and clone hT40-∆C and purified as described (21).”
Method
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
FTDP-17 Mutations in Tau Alter the Regulation of Microtubule Dynamics
LeBoeuf, A. C., Levy, S. F., Gaylord, M. A., Bhattacharya, A., Singh, A. K., Jordan, M. A., Wilson, L., & Feinstein, S. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803519200 · Cited by 46
Altered conformation of recombinant frontotemporal dementia-17 mutant tau proteins.
Jicha, G. A., Rockwood, J. M., Berenfeld, B., Hutton, M., & Davies, P. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00980-x · Cited by 44
Microtubule-associated protein tau in human fibroblasts with the Swedish Alzheimer mutation
Ingelson, M., Vanmechelen, E., & Lannfelt, L. (1996) · Neuroscience Letters · doi:10.1016/s0304-3940(96)13218-3 · Cited by 44
The association of tissue transglutaminase with human recombinant tau results in the formation of insoluble filamentous structures.
Appelt, D., & Balin, B. (1997) · Brain Research · doi:10.1016/s0006-8993(96)01121-3 · Cited by 47
Astrocytic accumulation of tau fibrils isolated from Alzheimer’s disease brains induces inflammation, cell-to-cell propagation and neuronal impairment
Eltom, K., Mothes, T., Libard, S., Ingelsson, M., & Erlandsson, A. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01745-8 · Cited by 46
“Samples were then loaded on 4–12% Bolt™ Bis-Tris Plus protein gels (Invitrogen, NW04125BOX), along with 5 µl PageRuler™ Plus Prestained Protein Lad-der (Thermo Fisher, 26,619).”
BackgroundMethodInfluential
Tau Isoform with Three Microtubule Binding Domains is a Marker of New Axons Generated from the Subgranular Zone in the Hippocampal Dentate Gyrus: Implications for Alzheimer's Disease
Llorens-Martı́n, M., Teixeira, C. M., Fuster-Matanzo, A., Jurado‐Arjona, J., Borrell, V., Soriano, E., Ávila, J., & Hernández, F. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-112057 · Cited by 51
“The 4R-Tau isoforms promote microtubule assembly at a faster rate than the 3R-Tau isoforms [27], suggesting that 3R-Tau protein may aid brain development by decreasing microtubule stability.”
Background
Structural disorder in four-repeat Tau fibrils reveals a new mechanism for barriers to cross-seeding of Tau isoforms
Weismiller, H. A., Murphy, R., Wei, G., Ma, B., Nussinov, R., & Margittai, M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005316 · Cited by 44
“The isoforms from each group are expressed at similar levels (19), and all of them are deposited into fibrils in AD (20).”
Background
Impaired tau–microtubule interactions are prevalent among pathogenic tau variants arising from missense mutations
Xia, Y., Sorrentino, Z. A., Kim, J. D., Strang, K. H., Riffe, C. J., & Giasson, B. I. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010178 · Cited by 48
Neurochemical approaches of cerebrospinal fluid diagnostics in neurodegenerative diseases
Otto, M., Lewczuk, P., & Wiltfang, J. (2008) · Methods · doi:10.1016/j.ymeth.2007.06.012 · Cited by 44
FTDP‐17 tau mutations decrease the susceptibility of tau to calpain I digestion
Yen, S. H., Easson, C., Nacharaju, P., Hutton, M. L., & Yen, S.-H. C. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01427-1 · Cited by 44
Characterisation of tau in the human and rodent enteric nervous system under physiological conditions and in tauopathy
Lionnet, A., Wade, M. A., Corbillé, A.-G., Prigent, A., Paillusson, S., Tasselli, M., Gonzales, J. A., Durieu, E., Rolli‐Derkinderen, M., Coron, E., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0568-3 · Cited by 45
Novel G335V mutation in the tau gene associated with early onset familial frontotemporal dementia
Neumann, M., Diekmann, S., Bertsch, U., Vanmassenhove, B., Bogerts, B., & Kretzschmar, H. A. (2005) · Neurogenetics · doi:10.1007/s10048-005-0210-y · Cited by 43
“Wild-type and mutant tau proteins were expressed in Escherichia coli BL21(DE3) as described previously [14].”
New insights into genetic and molecular mechanisms of brain degeneration in tauopathies
Forman, M. S., Lee, V. M. ‐., & Trojanowski, J. Q. (2000) · Journal of Chemical Neuroanatomy · doi:10.1016/s0891-0618(00)00100-9 · Cited by 43
In situ hybridization of calcium/calmodulin dependent protein kinase II and tau mRNAs: species differences and relative preservation in Alzheimer's disease
Mah, V. H., Eskin, T. A., Kazee, A. M., Lapham, L. W., & Higgins, G. A. (1992) · Molecular Brain Research · doi:10.1016/0169-328x(92)90071-i · Cited by 43
To target Tau pathologies, we must embrace and reconstruct their complexities
Limorenko, G., & Lashuel, H. A. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105536 · Cited by 41
Myotonic dystrophy 1 in the nervous system: From the clinic to molecular mechanisms
de León, M. B., & Cisneros, B. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21377 · Cited by 42
“Tau pre-mRNA is alternatively spliced at exons 2, 3, and 10 (Goedert et al., 1989b) producing in the adult human central nervous system six different mRNA isoforms that differ from each other by the inclusion or exclusion of these exons (Goedert et al., 1988, 1989a; Goedert and Jakes, 1990).”
Background
A double-labeling immunohistochemical study of tau exon 10 in Alzheimer's disease, progressive supranuclear palsy and Pick's disease
Ishizawa, K., Ksiȩżak-Reding, H., Davies, P., Delacourte, A., Tiseo, P. J., Yen, S. H., & Dickson, D. W. (2000) · Acta Neuropathologica · doi:10.1007/s004019900177 · Cited by 42
The Prion-Like Behavior of Assembled Tau in Transgenic MicePreprint
Clavaguera, F., Tolnay, M., & Goedert, M. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024372 · Cited by 45
“The C-terminal repeats (residues 252-376) and some adjoining sequences form the microtubule-binding domains of tau, with four-repeat isoforms (4R tau) being better at promoting microtubule assembly than isoforms with three repeats (3R tau) (Goedert and Jakes 1990).”
BackgroundSelf-citation
Closing the tau loop: the missing tau mutation
McCarthy, A. J., Lonergan, R. M., Olszewska, D. A., O’Dowd, S., Cummins, G. A., Magennis, B., Fallon, E., Pender, N. P., Huey, E. D., Cosentino, S., et al. (2015) · Brain · doi:10.1093/brain/awv234 · Cited by 41

Authors: Goedert, M., & Jakes, R.
Affiliations: MRC Laboratory of Molecular Biology (GB)
ORCID: Goedert, M.
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1990-12-01
Volume: 9
Issue: 13
Pages: 4225-4230
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1002/j.1460-2075.1990.tb07870.x
PMC: PMC552204
OpenAlex: W1509571186
Cited by: 929
References: 46
Citations by year: 2026: 23 · 2025: 29 · 2024: 50 · 2023: 39 · 2022: 40 · 2021: 53 · 2020: 34 · 2019: 39 · 2018: 42 · 2017: 41 · 2016: 27 · 2015: 37 · 2014: 18 · 2013: 21 · 2012: 25
FWCI: 15.03
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: tau protein, tau isoforms, microtubule-associated proteins, microtubule assembly, tandem repeats, recombinant protein expression, cerebral cortex, fetal brain
MeSH terms: Aged, Alkaline Phosphatase, Alzheimer Disease, Amino Acid Sequence, Brain, Escherichia coli, Humans, Isomerism, Microtubule-Associated Proteins, Middle Aged, Molecular Sequence Data, Recombinant Proteins, Repetitive Sequences, Nucleic Acid, RNA Splicing, RNA, Messenger, Tubulin, Mutagenesis, Site-Directed, tau Proteins

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Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.

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