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Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.
Open accessAbstract
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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“Since tau binds to microtubules through C-terminal repeats within the microtubule-binding domain, 4R tau isoforms show a higher propensity to promote microtubule assembly compared to 3R tau isoforms [122, 123].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [123]
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Cites
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
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311
[6] Use of T7 RNA polymerase to direct expression of cloned genes
Studier, F. W., Rosenberg, A. H., Dunn, J. J., & Dubendorff, J. W. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)85008-c · Cited by 6,562
Matsudaira, P. T. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61070-1 · Cited by 4,951
A protein factor essential for microtubule assembly
Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492
Self-citationMicrotubule-associated protein tau. A component of Alzheimer paired helical filaments.
Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780
The distribution of tau in the mammalian central nervous system.
Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1985) · The Journal of cell biology · doi:10.1083/jcb.101.4.1371 · Cited by 1,588
Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,491
Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4051 · Cited by 1,134
Self-citation
Research works printed but not linked: 7
- Goedert,M., Wischik,C.M., Crowther,R.A., Walker,J.E. and Klug,A. (1988) Proc. Natl. Acad. Sci. USA, 85, 4051-4055.
- Hirel,P.H., Schmitter,J.M., Dessen,P., Fayat,G. and Blanquet,S. (1989) Proc. Natl. Acad. Sci. USA, 86, 8247-8251.
- Kosik,K.S., Joachim,C.L. and Selkoe,D.J. (1986) Proc. Natl. Acad. Sci. USA, 83, 4044-4048.
- Weingarten,M.D., Lockwood,A.H., Hwo,S.Y. and Kirschner,M.W. (1975) Proc. Natl. Acad. Sci. USA, 72, 1858-1862.
- Wischik,C.M., Novak,M., Th0gersen,H.C., Edwards,P.C., Runswick,M.J., Jakes,R., Walker,J.E., Milstein,C., Roth,M. and Klug,A. (1988a) Proc. Natl. Acad. Sci. USA, 85, 4506-4510.
- Wischik,C.M., Novak,M., Edwards,P.C., Klug,A., Tichelaar,W. and Crowther,R.A. (1988b) Proc. Natl. Acad. Sci. USA, 85, 4884-4888.
- Wood,J.G., Mirra,S.S., Pollock,N.J. and Binder,L.I. (1986) Proc. Natl. Acad. Sci. USA, 83, 4040-4043. Received on August 28, 1990 4230 14602075, 1990, 13, Downloaded from https://www.embopress.org/doi/10.1002/j.1460-2075.1990.tb07870.x by Readcube (Labtiva Inc.), Wiley Online Library on [14/08/2023]. See the Terms and Conditions (https://onlinelibrary.wiley.com/terms-and-conditions) on Wiley Online Library for rules of use; OA articles are governed by the applicable Creative Commons License · DOI
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Cellular and pathological heterogeneity of primary tauopathies
Chung, D. C., Roemer, S. F., Petrucelli, L., & Dickson, D. W. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00476-x · Cited by 232
Tau alteration and neuronal degeneration in tauopathies: mechanisms and models
Brandt, R., Hundelt, M., & Shahani, N. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.018 · Cited by 235
“In adult human brain, the ratio of 3R tau to 4R tau isoforms is about one and the 1N, 0N, and 2N tau isoforms comprise about 54%, 37%, and 9%, respectively, of total tau [7].”
BackgroundTau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies
Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220
Novák, M., Jakes, R., Edwards, P. C., Milstein, C., & Wischik, C. M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.13.5837 · Cited by 219
Self-citationGoedert, M., & Spillantini, M. G. (2017) · Molecular Brain · doi:10.1186/s13041-017-0298-7 · Cited by 213
“Similar amounts of 3R and 4R Tau are expressed in the cerebral cortex of adults [16].”
BackgroundSelf-citationAtypical, non-standard functions of the microtubule associated Tau protein
Sotiropoulos, I., Galas, M., Silva, J. M., Skoulakis, E. M. C., Wegmann, S., Maina, M. B., Blum, D. L., Sayas, C. L., Mandelkow, E., Mandelkow�, E., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0489-6 · Cited by 221
“Expression of the six Tau isoforms is developmentally regulated [35], with the smallest and most highly phosphorylated 0N3R (352 a.”
BackgroundTransgenic Mouse Model of Tau Pathology in Astrocytes Leading to Nervous System Degeneration
Forman, M. S., Lal, D., Zhang, B., Dabir, D. V., Swanson, E., Lee, V. M.-Y., & Trojanowski, J. Q. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.0081-05.2005 · Cited by 198
“T34, one of the most abundant tau isoforms, contains both exon 2, the first of two alternatively spliced N-terminal exons, and exon 10, encoding for the second of four microtubule-binding repeats that is also alternatively spliced (Goedert and Jakes, 1990).”
BackgroundMethodInfluentialFTDP-17 mutations N279K and S305N in tau produce increased splicing of exon 10
Hasegawa, M., Smith, M. J., Iijima, M., Tabira, T., & Goedert, M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01696-2 · Cited by 184
Self-citationcAMP-Dependent Protein Kinase Phosphorylations on Tau in Alzheimer’s Disease
Jicha, G. A., Weaver, C. L., Lane, E., Vianna, C., Kress, Y., Rockwood, J. M., & Davies, P. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-17-07486.1999 · Cited by 207
“…has been shown to decrease the affinity of tau for microtubules leading to disruption of the neuronal cytoskeleton and axonal transport mechanisms (Goedert and Jakes, 1990; Drechsel et al., 1992; Raffaelli et al., 1992; Biernat et al., 1993; for review, see Lee, 1993; Scott et al., 1993; Yoshida…”
BackgroundDoes Alzheimer's disease begin in the brainstem?
Simic, G., Stanic, G., Mladinov, M., Jovanov‐Milosevic, N., Kostovic, I., & Hof, P. R. (2009) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2009.01038.x · Cited by 204
Cytosolic Fc receptor TRIM21 inhibits seeded tau aggregation
McEwan, W. A., Falcon, B., Vaysburd, M., Clift, D., Oblak, A. L., Ghetti, B., Goedert, M., & James, L. C. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1607215114 · Cited by 201
Self-citationBrion, J., Smith, C. J., Couck, A., Gallo, J., & Anderton, B. H. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07444.x · Cited by 202
Lovestone, S., Hartley, C. L., Pearce, J., & Anderton, B. H. (1996) · Neuroscience · doi:10.1016/0306-4522(96)00126-1 · Cited by 201
Tapia‐Rojas, C., Cabezas-Opazo, F., Deaton, C. A., Vergara, E. H., Johnson, G. V. W., & Quintanilla, R. A. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.005 · Cited by 207
“The different N-terminal inserts apparently do not affect microtubule assembly (Goedert and Jakes, 1990); but a recently study proposed that the Nterminal region could regulate microtubule stabilization.”
BackgroundInfluentialArai, T., Ikeda, K., Akiyama, H., Shikamoto, Y., Tsuchiya, K., Yagishita, S., Beach, T. G., Rogers, J., Schwab, C., & McGeer, P. L. (2001) · Acta Neuropathologica · doi:10.1007/s004010000283 · Cited by 197
Microtubule bundling by tau proteins in vivo: analysis of functional domains
Kanai, Y., Chen, J., & Hirokawa, N. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05489.x · Cited by 194
Tau protein, the paired helical filament and Alzheimer's disease
Goedert, M., Klug, A., & Crowther, R. A. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s323 · Cited by 205
“These findings, which were published at the end of 1990 [37], showed that the three repeat-containing isoform with no inserts is the major foetal form of human tau and that isoforms with three and four repeats,with and without amino-terminal inserts, are expressed in adult brain.”
Self-citationRoy, R. G., Mandal, P. K., & Maroon, J. C. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00486 · Cited by 194
The cytoskeleton in neurodegenerative diseases
Cairns, N. J., Lee, V. M. ‐., & Trojanowski, J. Q. (2004) · The Journal of Pathology · doi:10.1002/path.1650 · Cited by 193
“Another subset of the tau mutations has no effect on tau splicing, but instead alters the ability of tau to interact with MTs: missense mutations K257T, G272V, K280, N296, P301L, P301S, V337M, G389R, and R406W reduce the binding of tau to MTs and decrease its ability to promote MT stability and assembly in vitro [20,2…”
BackgroundAlternative splicing in neurodegenerative disease and the promise of RNA therapies
Nikom, D., & Zheng, S. (2023) · Nature reviews. Neuroscience · doi:10.1038/s41583-023-00717-6 · Cited by 201
Bourdenx, M., Koulakiotis, N. S., Sanoudou, D., Bézard, E., Dehay, B., & Tsarbopoulos, A. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.07.003 · Cited by 202
“In normal human brain tissue, the ratio between three repeats (3R) or four repeats (4R) is around 1 although this ratio is not conserved upon evolution despite a conserved exon organization (Andreadis et al., 1992; Goedert and Jakes, 1990; Kosik et al., 1989).”
BackgroundTau gene mutation in familial progressive subcortical gliosis
Goedert, M., Spillantini, M. G., Crowther, R. A., Chen, S. G., Parchi, P., Tabaton, M., Lanska, D. J., Markesbery, W. R., Wilhelmsen, K. C., Dickson, D. W., et al. (1999) · Nature Medicine · doi:10.1038/7454 · Cited by 187
Self-citationInteraction of tau protein with the dynactin complex
Magnani, E., Fan, J., Gasparini, L., Golding, M., Williams, M., Schiavo, G., Goedert, M., Amos, L., & Spillantini, M. G. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601878 · Cited by 205
Self-citationNisbet, R. M., Van der Jeugd, A., Leinenga, G., Evans, H. T., Janowicz, P. W., & Götz, J. (2017) · Brain · doi:10.1093/brain/awx052 · Cited by 187
“In the adult human brain, 2N tau is under-represented compared to the 0N and 1N isoforms and is estimated to comprise 9% of total tau (Goedert and Jakes, 1990).”
Ultrastructure and biochemical composition of paired helical filaments in corticobasal degeneration.
Ksiȩżak-Reding, H., Morgan, K., Mattiace, L. A., Davies, P., Liu, W. K., Yen, S. H., Weidenheim, K. M., & Dickson, D. W. (1994) · PubMed Central · Cited by 183
Walton, J. R. (2007) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2007.06.001 · Cited by 183
Tau isoform regulation is region‐ and cell‐specific in mouse brain
McMillan, P., Korvatska, E., Poorkaj, P., Evstafjeva, Z., Robinson, L., Greenup, L., Leverenz, J., Schellenberg, G. D., & D'Souza, I. (2008) · Journal of Comparative Neurology · doi:10.1002/cne.21867 · Cited by 179
Ferreira, A., Lu, Q., Orecchio, L., & Kosik, K. S. (1997) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1997.0615 · Cited by 178
Tau Proteins and Neurofibrillary Degeneration
Goedert, M., Spillantini, M. G., & Crowther, R. A. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00671.x · Cited by 178
Self-citationTau gene mutations: dissecting the pathogenesis of FTDP-17
Ingram, E., & Spillantini, M. G. (2002) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(02)02440-1 · Cited by 177
Kotzbauer, P. T. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.01.007 · Cited by 182
Jämsä, A., Hasslund, K., Cowburn, R. F., Bäckström, A., & Vasänge, M. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.05.075 · Cited by 171
Goedert, M. (1999) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.1999.0466 · Cited by 180
“In adult human brain, six isoforms of tau are expressed, which are produced by alternative mRNA splicing from a single gene located on the long arm of chromosome 17 (¢gure 3) (Goedert et al. 1989a,b; Goedert & Jakes 1990; Andreadis et al. 1992).”
BackgroundSelf-citationHereditary Frontotemporal Dementia Caused by Tau Gene Mutations
Van Swieten, J., & Spillantini, M. G. (2007) · Brain Pathology · doi:10.1111/j.1750-3639.2007.00052.x · Cited by 195
“In adult human brain, the ratio between three- and four-repeat tau isoforms is close to 1 (27).”
BackgroundTau mutations in frontotemporal dementia FTDP-17 and their relevance for Alzheimer’s disease
Goedert, M., & Spillantini, M. G. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00037-5 · Cited by 175
Self-citationLee, G. S., & Leugers, C. J. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00004-7 · Cited by 173
Zhang, S., Edelmann, L., Liu, J., Crandall, J. E., & Morabito, M. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.1900-07.2008 · Cited by 172
“It is interesting that in adult human brain, the ratio of 3R-tau to 4R-tau isoforms is about 1 [43].”
BackgroundCrowther, R. A., Olesen, O. F., Jakes, R., & Goedert, M. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81094-3 · Cited by 167
Self-citationAntisense oligonucleotides: treating neurodegeneration at the level of RNA
DeVos, S. L., & Miller, T. M. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0194-5 · Cited by 164
“In normal human brain, there is a 1:1 ratio of 4R:3R tau isoforms [94, 95], though mutations in tau can lead to a high 4R:3R ratio [96, 97], implicating 4R tau in the disease pathogenesis.”
BackgroundAmyloidogenesis of Tau protein
Niżyński, B., Dzwolak, W., & Nieznański, K. (2017) · Protein Science · doi:10.1002/pro.3275 · Cited by 166
“range from 352 to 441 amino acid residues in length.(35) Each Tau isoform contains a projection”
BackgroundTau and transgenic animal models
Götz, J. (2001) · Brain Research Reviews · doi:10.1016/s0165-0173(01)00055-8 · Cited by 166
TauGene Mutation K257T Causes a Tauopathy Similar to Pick's Disease
Rizzini, C., Goedert, M., Hodges, J. R., Smith, M. J., Jakes, R., Hills, R., Xuereb, J. H., Crowther, R. A., & Spillantini, M. G. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.11.990 · Cited by 161
“Dephosphorylation and immunoblotting were done as described (7).”
BackgroundMethodInfluentialSelf-citationFamilial frontotemporal dementia with ubiquitin-positive inclusions is linked to chromosome 17q21-22
Rosso, S. M. (2001) · Brain · doi:10.1093/brain/124.10.1948 · Cited by 158
“Soluble tau was extracted with 2.5% perchloric acid as described previously (Goedert and Jakes, 1990 M ϭ male; F ϭ female; FT ϭ frontotemporal; T ϭ temporal; FϾT ϭ frontal atrophy more severe than temporal atrophy; R ϭ right; L ϭ left; NA ϭ not available.”
MethodInfluentialIsoforms changes of tau protein during development in various species
Takuma, H., Arawaka, S., & Mori, H. (2003) · Developmental Brain Research · doi:10.1016/s0165-3806(03)00056-7 · Cited by 157
EVANS, D. B., Rank, K. B., Bhattacharya, K., Thomsen, D. R., Gurney, M. E., & Sharma, S. K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000808200 · Cited by 155
Buée‐Scherrer, V., Condamines, O., Mourton-Gilles, C., Jakes, R., Goedert, M., Pau, B., & Delacourte, A. (1996) · Molecular Brain Research · doi:10.1016/0169-328x(96)00003-4 · Cited by 161
“Recombinant tau proteins were purified by an improvement [8] of the procedure described in [17].”
MethodSelf-citationGenetics of FTLD : overview and what else we can expect from genetic studies
Pottier, C., Ravenscroft, T. A., Sanchez‐Contreras, M., & Rademakers, R. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13622 · Cited by 148
“With respect to MT assembly, it has been shown that 4R tau binds to MT threefold more strongly and assembles MT more efficiently than 3R tau (Goedert & Jakes 1990).”
BackgroundAssembly of Alzheimer‐like filaments from full‐length tau protein
Crowther, R. A., Olesen, O. F., Smith, M. J., Jakes, R., & Goedert, M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80260-2 · Cited by 154
Self-citationAlzheimer paired helical filaments Restoration of the biological activity by dephosphorylation
Iqbal, K., Zaidi, T., Bancher, C., & Grundke, I. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00650-4 · Cited by 150
Identification of 3‐ and 4‐repeat tau isoforms within the PHF in Alzheimer's disease.
Jakes, R., Novák, M., Davison, M., & Wischik, C. M. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07820.x · Cited by 151
Self-citationSposito, T., Preza, E., Mahoney, C. J., Setó-Salvia, N., Ryan, N. S., Morris, H. R., Arber, C., Devine, M. J., Houlden, H., Warner, T. T., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv246 · Cited by 148
“below the limit of detection in our analysis (7,8).”
BackgroundPrion-like Mechanisms in the Pathogenesis of Tauopathies and Synucleinopathies
Goedert, M., Falcon, B., Clavaguera, F., & Tolnay, M. (2014) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-014-0495-z · Cited by 152
Self-citationAxonal transport, tau protein, and neurodegeneration in Alzheimer's disease
Terwel, D., Dewachter, I., & Van Leuven, F. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:2:2:151 · Cited by 146
“It is to be remembered that tau protein with four C-terminal domains (tau-4R) binds more tightly to microtubules than three-repeat tau (tau-3R) (Goedert and Jakes, 1990; Scott et al., 1991).”
BackgroundThe role of tau phosphorylation and cleavage in neuronal cell death
Chun, W. (2006) · Frontiers in bioscience · doi:10.2741/2097 · Cited by 144
“In adult human brain, the ratio of 3R tau to 4R tau isoforms is about one and the 1N, 0N, and 2N isoforms comprise about 54%, 37%, and 9%, respectively, of total tau (28).”
BackgroundVaquer‐Alicea, J., Diamond, M. I., & Joachimiak, Ł. A. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02301-7 · Cited by 139
Buchholz, S., & Zempel, H. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13784 · Cited by 154
“74,112–114, 132–”
BackgroundDistribution of the phosphorylated microtubule-associated protein tau in developing cortical neurons
Brion, J., Octave, J., & Couck, A. M. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90533-9 · Cited by 143
Mawal-Dewan, M., Henley, J., VOORDE, A. V. D., Trojanowski, J. Q., & Lee, V. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47378-4 · Cited by 140
A role for FKBP52 in tau protein function
Chambraud, B., Sardin, E., Giustiniani, J., Dounane, O., Schumacher, M., Goedert, M., & Baulieu, E.-E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914957107 · Cited by 140
“colifromclones hT40, hT39, hT37, hT34, hT24, hT23 and purified as described (21).”
BackgroundMethodSelf-citationThe role of tau in the pathological process and clinical expression of Huntington’s disease
Vuono, R., Winder‐Rhodes, S., de Silva, R., Cisbani, G., Drouin‐Ouellet, J., REGISTRY Investigators of the European Huntington’s Disease Network, Spillantini, M. G., Cicchetti, F., & Barker, R. A. (2015) · Brain · doi:10.1093/brain/awv107 · Cited by 139
“Preparation of soluble and insoluble tau fractions from Huntington’s disease, tauopathy and control brains was adapted from previously published methods (Goedert et al., 1989; Goedert and Jakes, 1990; Hanger et al., 2002).”
The proline-rich domain of tau plays a role in interactions with actin
He, H. J., Wang, X. S., Pan, R., Wang, D. L., Liu, M. N., & He, R. Q. (2009) · BMC Cell Biology · doi:10.1186/1471-2121-10-81 · Cited by 142
“The shortest isoform of human tau (tau23) was purified with Q-Sepharose and SP-Sepharose chromatography (Amersham Pharmacia Biotech, Switzerland) as described by Goedert and Jakes [28].”
MethodDifferential effect of three‐repeat and four‐repeat tau on mitochondrial axonal transport
Stoothoff, W., Jones, P. B., Spires‐Jones, T. L., Joyner, D., Chhabra, E., Bercury, K., Fan, Z., Xie, H., Bacskai, B., Edd, J., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06316.x · Cited by 135
Microtubule-associated proteins and neuronal morphogenesis
Matus, A. I. (1991) · Journal of Cell Science · doi:10.1242/jcs.1991.supplement_15.9 · Cited by 138
Biosensors for Alzheimer's disease biomarker detection: A review
Shui, B., Tao, D., Florea, A., Cheng, J., Zhao, Q., Gu, Y., Li, W., Jaffrezic-Renault, N. J., Mei, Y., & Guo, Z. (2018) · Biochimie · doi:10.1016/j.biochi.2017.12.015 · Cited by 139
Normal and Pathological Tau Proteins as Factors for Microtubule Assembly
Delacourte, A., & Buée, L. (1997) · International review of cytology · doi:10.1016/s0074-7696(08)62588-7 · Cited by 145
Feijoo, C., Campbell, D. G., Jakes, R., Goedert, M., & Cuenda, A. (2005) · Journal of Cell Science · doi:10.1242/jcs.01655 · Cited by 133
“Recombinant hTau46 (a 412 amino acid isoform of human brain Tau) was expressed and purified as previously described (Goedert and Jakes, 1990).”
MethodSelf-citationPick's disease associated with the novel Tau gene mutation K369I
Neumann, M., Schulz‐Schaeffer, W., Crowther, R. A., Smith, M. J., Spillantini, M. G., Goedert, M., & Kretzschmar, H. A. (2001) · Annals of Neurology · doi:10.1002/ana.1223 · Cited by 134
“BL21(DE3), as previously described.(7) Tau proteins were purified and their concentrations determined by densitometry, as described.”
BackgroundMethodSelf-citationImpaired Glutamate Transport in a Mouse Model of Tau Pathology in Astrocytes
Dabir, D. V., Robinson, M. B., Swanson, E., Zhang, B., Trojanowski, J. Q., Lee, V. M. ‐., & Forman, M. S. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3861-05.2006 · Cited by 138
“For GFAP/tauP301L Tg mice, cDNA constructs containing the T34 (4R/1N) human tau isoform (Goedert and Jakes, 1990) was subcloned into the eukaryotic expression vector pGfa2 expression vector at the BamHI restriction site that uses the astrocyte-specific GFAP promoter (Brenner and Messing, 1996; Forman et al.”
Method“Prion‐Like” Templated Misfolding in Tauopathies
Clavaguera, F., Lavenir, I., Falcon, B., Frank, S., Goedert, M., & Tolnay, M. (2013) · Brain Pathology · doi:10.1111/bpa.12044 · Cited by 133
“The repeats and some adjoining sequences constitute the microtubule-binding domains of tau (43), with four-repeat tau being better at promoting microtubule assembly than tau with three repeats (38).”
BackgroundSelf-citationThe disordered neuronal cytoskeleton in Alzheimer's disease
Lee, V. M. ‐., & Trojanowski, J. Q. (1992) · Current Opinion in Neurobiology · doi:10.1016/0959-4388(92)90034-i · Cited by 129
Tau filaments in neurodegenerative diseases
Goedert, M. (2018) · FEBS Letters · doi:10.1002/1873-3468.13108 · Cited by 127
Self-citationThe role of exosomes in the pathogenesis of Alzheimer’ disease
Xiao, T., Zhang, W., Jiao, B., Pan, C., Liu, X., & Shen, L. H. (2017) · Translational Neurodegeneration · doi:10.1186/s40035-017-0072-x · Cited by 133
“An abnormal 3R/4R balance is thought to impair the function of tau in keeping stabilization of microtubule structure and material transport [70].”
BackgroundWest, R. R., Tenbarge, K. M., & Olmsted, J. B. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54720-7 · Cited by 127
Mutations in the tau gene that cause an increase in three repeat tau and frontotemporal dementia
Stanford, P. M. (2003) · Brain · doi:10.1093/brain/awg090 · Cited by 125
“The alternative splicing of exon 10 generates tau isoforms containing either three or four repeats of 31 or 32 amino acids (Goedert and Jakes, 1990).”
BackgroundMethodExpression of microtubule-associated proteins MAP2 and tau in cultured rat brain oligodendrocytes
Müller, R., Heinrich, M., Heck, S., Blohm, D., & Richter-Landsberg, C. (1997) · Cell and Tissue Research · doi:10.1007/s004410050809 · Cited by 127
“1989a,b) and are more potent in promoting tubulin polymerization in vitro (Goedert and Jakes 1990).”
Phenotypic Heterogeneity of Monogenic Frontotemporal Dementia
Benussi, A., Padovani, A., & Borroni, B. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00171 · Cited by 129
“org microtubule-binding domains of tau, with 4R tau having greater predisposition for microtubule assembly than 3R tau (Goedert and Jakes, 1990).”
BackgroundSmall-molecule PET Tracers for Imaging Proteinopathies
Mathis, C. A., Lopresti, B. J., Ikonomović, M. D., & Klunk, W. E. (2017) · Seminars in Nuclear Medicine · doi:10.1053/j.semnuclmed.2017.06.003 · Cited by 124
Analysis of Tau Phosphorylation and Truncation in a Mouse Model of Human Tauopathy
Delobel, P., Lavenir, I., Fraser, G. M., Ingram, E., Holzer, M., Ghetti, B. F., Spillantini, M. G., Crowther, R. A., & Goedert, M. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2008.070627 · Cited by 124
“C–F: Decoration by Tau-C3 of a filament assembled from recombinant tau(1-421) (C), a paired helical filament (D), and a straight filament (E) from AD brain, as well as a ribbon-like filament (F) from a case of FTDP-17T with the P301L mutation in Tau.”
BackgroundSelf-citationGoedert, M., Baur, C.-P., Ahringer, J., Jakes, R., Hasegawa, M., Spillantini, M. G., Smith, M. J., & Hill, F. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.11.2661 · Cited by 123
Self-citationAccumulation of Filamentous Tau in the Cerebral Cortex of Human Tau R406W Transgenic Mice
Ikeda, M., Kawarai, T., Kawarabayashi, T., Matsubara, E., Murakami, T., Sasaki, A., Tomidokoro, Y., Ikarashi, Y., Kuribara, H., Ishiguro, K., et al. (2005) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)62274-2 · Cited by 120
Rudrabhatla, P., Jaffe, H., & Pant, H. C. (2011) · The FASEB Journal · doi:10.1096/fj.11-181297 · Cited by 121
“Six isoforms of tau exist in human brain (47), differing by the presence or absence of two types of amino acid insertion in the amino-terminal half of the molecule (inserts 1 and 2) and one of the amino acid insertion in the carboxy-terminal half of tau (48).”
BackgroundTau: The Center of a Signaling Nexus in Alzheimer's Disease
Khan, S. S., & Bloom, G. S. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00031 · Cited by 121
Esteras, N., Rohrer, J. D., Hardy, J., Wray, S., & Abramov, A. Y. (2017) · Redox Biology · doi:10.1016/j.redox.2017.03.008 · Cited by 120
“In a normal brain there is a similar proportion of 3R and 4R isoforms [13,23].”
BackgroundBiswas, S., & Kalil, K. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2281-17.2017 · Cited by 133
“Expression of different tau isoforms is developmentally regulated in both human and rodent brains in early development (Goedert et al., 1989; Kosik et al., 1989; Goedert and Jakes, 1990; Kampers et al., 1999; Takuma et al., 2003).”
BackgroundA comprehensive resource for induced pluripotent stem cells from patients with primary tauopathies
Karch, C. M., Kao, A. W., Karydas, A., Onanuga, K., Martinez, R., Argouarch, A., Wang, C., Huang, C., Sohn, P. D., Bowles, K. R., et al. (2019) · Stem Cell Reports · doi:10.1016/j.stemcr.2019.09.006 · Cited by 119
“While tau isoforms may share broad functional similarities, different isoforms likely play distinct physiological and pathological roles in the cell (Goedert and Jakes, 1990; Karch et al., 2012; Kosik et al., 1989; Panda et al., 2003).”
BackgroundDifferential Incorporation of Tau Isoforms in Alzheimer's Disease
Espinoza, M., de Silva, R., Dickson, D. W., & Davies, P. (2008) · Journal of Alzheimer's Disease · doi:10.3233/jad-2008-14101 · Cited by 119
“For example, it has been shown that 4R tau isoforms are more efficient at promoting microtubule assembly than 3R tau isoforms [20,23].”
New perspectives on the role of tau in Alzheimer's disease. Implications for therapy
Medina, M., & Ávila, J. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.013 · Cited by 123
“only expresses 3R tau, demonstrating developmental regulation of exon 10 splicing [7].”
Pathogenesis of the Tauopathies
Goedert, M., & Spillantini, M. G. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9593-4 · Cited by 126
Self-citationGarbern, J. Y., Neumann, M., Trojanowski, J. Q., Lee, V. M. ‐., Feldman, G. L., Norris, J. W., Friez, M. J., Schwartz, C. E., Stevenson, R. E., & Sima, A. A. F. (2010) · Brain · doi:10.1093/brain/awq071 · Cited by 117
“Splicing of exons 2, 3 and 10 is tightly regulated to maintain similar levels of 4R to 3R isoforms in the normal human brain (Goedert and Jakes, 1990).”
BackgroundPotential 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
“For instance, only one Tau isoform, characterized by 3R and no N-terminal inserts, is present during fetal stages, while the six isoforms (with one or two N-terminal inserts and 3 or 4R) are expressed during adulthood (Kosik et al., 1989; Goedert and Jakes, 1990).”
BackgroundSadik, G., Tanaka, T., Kato, K., Yamamori, H., Begum, N. N., Morihara, T., & Takeda, M. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05716.x · Cited by 114
“Tau in fetal brain has been shown to promote microtubule assembly less efficiently than tau in adult brain (Goedert and Jakes 1990) and the elevated level of phosphorylated tau in fetal brain correlates with the presence of dynamic microtubules during periods of high plasticity in the developing mammalian brain (Brion…”
BackgroundKalbfuss, B., Mabon, S. A., & Misteli, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105113200 · Cited by 114
Synphilin-1 is present in Lewy bodies in Parkinson's disease
Wakabayashi, K., Engelender, S., Yoshimoto, M., Tsuji, S., Ross, C. A., & Takahashi, H. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200004)47:4 · Cited by 269
Self-citationTau and Axonopathy in Neurodegenerative Disorders
Higuchi, M., Lee, V. M.-Y., & Trojanowski, J. Q. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:2:2:131 · Cited by 134
“0 times faster rate of MT assembly than 3RTs (Goedert and Jakes, 1990; Butner and Kirschner, 1991; Gustke et al., 1992).”
InfluentialDistinct Therapeutic Mechanisms of Tau Antibodies
Funk, K. E., Mirbaha, H., Jiang, H., Holtzman, D. M., & Diamond, M. I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.657924 · Cited by 111
“Recombinant 2N4R and RD Tau were prepared as described previously and stored lyophilized at 80 °C (24).”
MethodTau 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
Tau as a Biomarker of Neurodegeneration
Holper, S., Watson, R., & Yassi, N. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137307 · Cited by 121
“Terminal insert number is less evenly distributed: 1N, 0N and 2N isoforms account for 54%, 37% and 9%, respectively, of total brain tau [29].”
BackgroundInfluentialAlzheimer disease therapeutics: Focus on the disease and not just plaques and tangles
Iqbal, K., Liu, F., & Gong, C. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.002 · Cited by 114
“Adult human brain expresses approximately equal levels of 3R-tau and 4R-tau [95, 96].”
BackgroundProgressive supranuclear palsy: Advances in diagnosis and management
Coughlin, D. G., & Litvan, I. (2020) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2020.04.014 · Cited by 118
“Due to alternative splicing of the of microtubule binding site domains E2, E3, and E10, six tau isoforms exist, either with 4 repeated domains (4R, which includes the E10 region), or 3 repeated domains (3R, which excludes E10) [3].”
BackgroundBrion, J., Hanger, D. P., Couck, A. M., & Anderton, B. H. (1991) · Biochemical Journal · doi:10.1042/bj2790831 · Cited by 109
Metadata
- Authors
- Goedert, M., & Jakes, R.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- ORCID
- Goedert, M.
- Venue
- The EMBO Journal
- Published
- 1990-12-01
- Volume
- 9
- Issue
- 13
- Pages
- 4225-4230
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- 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
- 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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