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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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Chaperoning shape-shifting tau in disease
Ryder, B. D., Wydorski, P. M., Hou, Z., & Joachimiak, Ł. A. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.12.009 · Cited by 44
Bai, Q., & Burton, E. A. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.09.004 · Cited by 42
“4R-Tau binds to microtubules with greater avidity than 3R-Tau isoforms [4,11,12] (this is attributable to sequences in the first inter-repeat segment that are unique to 4R proteins, rather than to the additional copy of the microtubule-binding tandem repeat [13]), suggesting that expression of 4R-Tau may favor microtu…”
BackgroundTau Alternative Splicing and Frontotemporal Dementia
Kar, A. N., Kuo, D. C., He, R.-Q., Zhou, J., & Wu, J. Y. (2005) · Alzheimer Disease & Associated Disorders · doi:10.1097/01.wad.0000183082.76820.81 · Cited by 41
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Human stem cell-derived neurons: a system to study human tau function and dysfunction
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Tau and α-Synuclein Inclusions in a Case of Familial Frontotemporal Dementia and Progressive Aphasia
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“5% perchloric acid, as previously described (28).”
Induced pluripotent stem cell - derived neurons for the study of spinocerebellar ataxia type 3
Hansen, S. K., Stummann, T. C., Madsen, H. B., Hasholt, L., Tümer, Z., Nielsen, J. E., Rasmussen, M. A., Nielsen, T. T., Daechsel, J. C. A., Fog, K., et al. (2016) · Stem Cell Research · doi:10.1016/j.scr.2016.07.004 · Cited by 40
“In line with these observations, only the embryonic isoform of Tau 0N3R (Goedert and Jakes, 1990) was expressed.”
BackgroundMari, S. A., Wegmann, S., Tepper, K., Hyman, B. T., Mandelkow, E., Mandelkow�, E., & Müller, D. J. (2018) · Nano Letters · doi:10.1021/acs.nanolett.8b01085 · Cited by 39
Heparan Sulfate as a Therapeutic Target in Tauopathies: Insights From Zebrafish
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Lu, J., Bao, W., Li, M., Li, L., Zhang, Z., Alberts, I., Brendel, M., Cumming, P. D., Lu, H., Xiao, Z., et al. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00604 · Cited by 41
“In healthy adults, equal amounts of tau protein isoforms with three microtubule-binding domains (3R) and four microtubule-binding domains (4R) occur in the cerebral cortex (Goedert and Jakes, 1990).”
BackgroundGarver, T. D., Kincaid, R. L., Conn, R. A., & Billingsley, M. L. (1999) · PubMed · Cited by 40
Modulation of PHF-like tau phosphorylation in cultured neurones and transfected cells
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Caenorhabditis elegans models of tauopathy
Pir, G. J., Choudhary, B. C., & Mandelkow�, E. (2017) · The FASEB Journal · doi:10.1096/fj.201701007 · Cited by 39
“The number of repeats correlates with tau’s affinity for microtubules (15).”
BackgroundBinding Sites on Tau Proteins as Components for Antimicrobial Peptides
Kobayashi, N. B., MASUDA, J., Kudoh, J., Shimizu, N., & Yoshida, T. (2008) · Biocontrol Science · doi:10.4265/bio.13.49 · Cited by 39
The Alzheimer’s Disease Related Tau Protein as a New Target for Chemical Protein Engineering
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The Microtubule-Associated Protein Tau and Its Relevance for Pancreatic Beta Cells
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“The six MAPT isoforms (MAPT1 to MAPT6) expression is well documented in the human brain [39, 40].”
BackgroundDetection of all adult Tau isoforms in a 3D culture model of iPSC-derived neurons
Miguel, L., Rovelet‐Lecrux, A., Feyeux, M., Frébourg, T., Nassoy, P., Campion, D., & Lecourtois, M. (2019) · Stem Cell Research · doi:10.1016/j.scr.2019.101541 · Cited by 37
“The 2N species are underrepresented in comparison to 0N and 1N isoforms, such that 2N, 1N and 0N isoforms make up 9%, 54%, and 37% of the total, respectively (Goedert and Jakes, 1990; Hong et al., 1998).”
BackgroundResultThe Difference in the Binding of Phosphatidylinositol Distinguishes MAP2 from MAP2C and Tau
Surridge, C. D., & Burns, R. G. (1994) · Biochemistry · doi:10.1021/bi00192a009 · Cited by 39
Alternative splicing of exon 10 in the taugene as a target for treatment of tauopathies
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“It is interesting that in adult human brain, the ratio of 3R-tau to 4R-tau isoforms is about 1 [43].”
First one in, last one out: the role of GABAergic transmission in generation and degeneration
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The propagation mechanisms of extracellular tau in Alzheimer’s disease
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Yeast as a Model System to Study Tau Biology
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“In normal adult human tissue, the ratio of 4R- to 3R-Tau is ∼1 [21, 22].”
BackgroundTau isoform expression and regulation in human cortical neurons
Deshpande, A. M., Win, K. M., & Busciglio, J. A. (2008) · The FASEB Journal · doi:10.1096/fj.07-096909 · Cited by 41
“0N, 1N, and 2N isoforms is 37:54:9 (20, 21).”
Emerging Diagnostic and Therapeutic Strategies for Tauopathies
Coughlin, D. G., & Irwin, D. J. (2017) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-017-0779-1 · Cited by 42
“Initial studies in paclitaxel were affective in a tau murine model [148•] but may be limited by side effects from exposure to the peripheral nervous system at dosages that reach the CNS in humans; however, several later studies find related compounds with high blood brain barrier (BBB) permeability can ameliorate tau…”
BackgroundResultInfluentialThe human MAPT locus generates circular RNAs
Welden, J. R., van Doorn, J., Nelson, P. T., & Stamm, S. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.04.023 · Cited by 37
“Exon 10 encodes one of the four microtubule binding sites, and its alternative usage generates tau isoforms with either 3 or 4 binding sites (3R, 4R) that differ in their affinity to microtubules [5] and could thus ‘fine tune’ the interaction between the Tau protein and microtubules.”
BackgroundHuman tauopathy-derived tau strains determine the substrates recruited for templated amplification
Tarutani, A., Miyata, H., Nonaka, T., Hasegawa, K., Yoshida, M., Saito, Y., Murayama, S., Robinson, A., Mann, D. M. A., Tomita, T., et al. (2021) · Brain · doi:10.1093/brain/awab091 · Cited by 37
“tau (3R tau) and four-repeat tau (4R tau) isoforms according to the number of repeats (R1–R4) in the microtubule-binding domain, and the two types are expressed in the adult human brain at a ratio of 1:1.(4) Under physiological conditions, tau is localized mainly in axons as a soluble, natively unfolded protein, and f…”
BackgroundBehrstock, S. P., Anantharam, V., Thompson, K. W., Schweitzer, E. S., & Tobin, A. J. (2000) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(20000501)60:3 · Cited by 17
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The novel Tau mutation G335S: clinical, neuropathological and molecular characterization
Spina, S., Murrell, J. R., Yoshida, H., Ghetti, B. F., Bermingham, N., Sweeney, B. J., Dlouhy, S. R., Crowther, R. A., Goedert, M., & Keohane, C. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0182-5 · Cited by 37
Self-citationCryo-EM structures of pathogenic fibrils and their impact on neurodegenerative disease research
Todd, T. W., Islam, N. N., Cook, C. N., Caulfield, T. R., & Petrucelli, L. (2024) · Neuron · doi:10.1016/j.neuron.2024.05.012 · Cited by 37
Application of yeast to studying amyloid and prion diseases
Chernoff, Y. O., Grizel, A. V., Rubel, A. A., Zelinsky, A. А., Chandramowlishwaran, P., & Chernova, T. A. (2020) · Advances in genetics · doi:10.1016/bs.adgen.2020.01.002 · Cited by 41
Eteläinen, T. S., Silva, M. C., Uhari-Väänänen, J. K., Lorenzo, F. D., Jäntti, M. H., Cui, H., Chavero‐Pieres, M., Kilpeläinen, T. P., Mechtler, C., Svarcbahs, R., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abq2915 · Cited by 36
“Differences between these isoforms are the presence of three (3R) or four (4R) repeat domains in the C-terminal microtubule–binding region and the absence or presence of one or two inserts in the N-terminal projection region (0N, 1N, and 2N) (9).”
BackgroundDupré, E., Danis, C., Arrial, A., Hanoulle, X., Homa, M., Cantrelle, F., Merzougui, H., Colin, M., Rain, J., Buée, L., et al. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00217 · Cited by 37
Expression of GFAP and Tau Following Blast Exposure in the Cerebral Cortex of Ferrets
Schwerin, S. C., Chatterjee, M., Hutchinson, E. B., Djankpa, F. T., Armstrong, R. C., McCabe, J. T., Perl, D. P., & Juliano, S. L. (2021) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlaa157 · Cited by 34
“The human 3R and 4R isoforms of tau show expression in roughly equal amounts, but the ratio differs in a number of disease conditions (20, 25, 26).”
BackgroundHeterogeneity of tau proteins during mouse brain development and differentiation of cultured neurons
Larcher, J. C., Boucher, D., Ginzburg, I., Gros, F., & Denoulet, P. (1992) · Developmental Biology · doi:10.1016/0012-1606(92)90059-p · Cited by 35
Expression and phosphorylation of a three-repeat isoform of tau in transfected non-neuronal cells
Gallo, J., Hanger, D. P., Twist, E. C., Kosik, K. S., & Anderton, B. H. (1992) · Biochemical Journal · doi:10.1042/bj2860399 · Cited by 35
Tau proteinopathies and the prion concept
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Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology
Berrocal, M., Corbacho‐Cuello, I., Vázquez-Hernández, M., Ávila, J., Sepúlveda, M. R., & Mata, A. M. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.04.007 · Cited by 34
“coli containing 2 N-terminal inserts and 4 microtubule binding repeats, that is usually named as tau 42 according to [32].”
BackgroundIovino, M., Pfisterer, U., Holton, J. L., Lashley, T., Swingler, R. J., Calò, L., Treacy, R., Révész, T., Parmar, M., Goedert, M., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1219-1 · Cited by 33
“the ability of recombinant tau proteins to promote microtubule assembly was monitored by turbidity, as described [8].”
MethodSelf-citationPeck, A. J., Sargin, M. E., LaPointe, N. E., Rose, K. H., Manjunath, B. S., Feinstein, S. C., & Wilson, L. (2010) · Cytoskeleton · doi:10.1002/cm.20494 · Cited by 34
“4R tau generally exhibits higher levels of MT assembly promoting and dynamics regulatory activities than 3R tau [Goedert and Jakes, 1990; Trinczek et al., 1995; Goode et al., 2000; Panda et al., 2003; Bunker et al., 2004; Levy et al., 2005].”
BackgroundUncovering specificity of endogenous TAU aggregation in a human iPSC-neuron TAU seeding model
Manos, J. D., Preiss, C. N., Venkat, N., Tamm, J., Reinhardt, P., Kwon, T., Wu, J., Winter, A. D., Jahn, T. R., Yanamandra, K., et al. (2022) · iScience · doi:10.1016/j.isci.2021.103658 · Cited by 36
Involvement of glycogen synthase kinase‐3β and tau phosphorylation in neuronal Golgi disassembly
Elyaman, W., Yardin, C., & Hugon, J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00838.x · Cited by 34
“The affinity of tau for MTs is regulated by (i) the number of MT binding repeats (Goedert and Jakes 1990); (ii) the proline-rich sequence adjacent to the MT binding domain (Gustke et al.”
BackgroundSite-specific regulation of Alzheimer-like tau phosphorylation in living neurons
Burack, M. A., & Halpain, S. (1996) · Neuroscience · doi:10.1016/0306-4522(95)00546-3 · Cited by 36
Yanagawa, H., Chung, S.-H., Ogawa, Y., Sato, K., Shibata‐Seki, T., Masai, J., & Ishiguro, K. (1998) · Biochemistry · doi:10.1021/bi9724265 · Cited by 34
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Tau Protein and Frontotemporal Dementias
Goedert, M., Spillantini, M. G., Falcon, B., Zhang, W., Newell, K. L., Hasegawa, M., Scheres, S. H. W., & Ghetti, B. F. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-51140-1_12 · Cited by 37
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“forms is about one in normal brains, with 4R exhibiting higher affinity for microtubules than 3R in vitro (4).”
BackgroundPharmacological Modulators of Tau Aggregation and Spreading
Dominguez‐Meijide, A., Vasili, E., & Outeiro, T. F. (2020) · Brain Sciences · doi:10.3390/brainsci10110858 · Cited by 36
“Three repeat tau isoforms bind microtubules less e ff ectively than isoforms with four repeats, probably due to the presence of the interrepeat sequence between the first and second microtubule binding domains, which is unique to 4R isoforms [45].”
BackgroundThe tau mutation (val337met) disrupts cytoskeletal networks of microtubules
Arawaka, S., Usami, M., Sahara, N., Schellenberg, G. D., Lee, G. S., & Mori, H. (1999) · Neuroreport · doi:10.1097/00001756-199904060-00018 · Cited by 33
The role of tau phosphorylation in transfected COS-1 cells
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Differential distribution of tau proteins in developing cat cerebellum
Riederer, B. M., & Binder, L. I. (1994) · Brain Research Bulletin · doi:10.1016/0361-9230(94)90245-3 · Cited by 33
Tau Protein in Frontotemporal Dementia Linked to Chromosome 3 (FTD-3)
Yancopoulou, D., Crowther, R. A., Chakrabarti, L., Gydesen, S., Brown, J., & Spillantini, M. G. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.8.878 · Cited by 33
“Sarkosyl-insoluble tau was extracted from the frontal cortex of II-12 and J Neuropathol Exp Neurol, Vol 62, August, 2003 it appeared as 3 major bands of 60, 64, and 68 kDa following immunoblotting with tau antiserum BR133 (Fig.”
MethodInfluentialNeurochemical Profile of Dementia Pugilistica
Kokjohn, T. A., Maarouf, C. L., Daugs, I. D., Hunter, J. M., Whiteside, C. M., Malek-Ahmadi, M., Rodriguez, E., Kalback, W., Jacobson, S. A., Sabbagh, M. N., et al. (2013) · Journal of Neurotrauma · doi:10.1089/neu.2012.2699 · Cited by 39
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“For example, in the normal human brain, the ratio of tau-4R to tau-3R is approximately 1; this balanced isoform ratio appears to be essential for proper neuronal function [17,18].”
Tau Filaments and the Development of Positron Emission Tomography Tracers
Goedert, M., Yamaguchi, Y., Mishra, S. K., Higuchi, M., & Sahara, N. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00070 · Cited by 32
Self-citationThree‐repeat and four‐repeat tau isoforms form different oligomers
Shahpasand‐Kroner, H., Portillo, J., Lantz, C., Seidler, P. M., Sarafian, N., Loo, J. A., & Bitan, G. (2021) · Protein Science · doi:10.1002/pro.4257 · Cited by 32
“In the adult human brain, the proportion of 3R and 4R tau isoforms are roughly equal and 0N, 1N, and 2N comprise 37, 54, and 9% of total tau, respectively.(39) Thus, we tested whether the TOC1-reactivity of a mixture of all the isoforms in these proportions would simply reflect the oligomerization of each isoform or w…”
BackgroundCHAMBERS, J. K., Uchida, K., Harada, T., Tsuboi, M., Sato, M., Kubo, M., Kawaguchi, H., Miyoshi, N., Tsujimoto, H., & Nakayama, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046452 · Cited by 31
Chukwu, J. E., Pedersen, J. T., Pedersen, L. Ø., Volbracht, C., Sigurdsson, E. M., & Kong, X. (2018) · Scientific Reports · doi:10.1038/s41598-018-24276-4 · Cited by 32
Lu, X., & Ferreira, P. A. (2005) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.04-1286 · Cited by 32
Breuzard, G., Pagano, A., Bastonero, S., Malesinski, S., Parat, F., Barbier, P., Peyrot, V., & Kovacic, H. (2019) · Journal of Cell Science · doi:10.1242/jcs.222851 · Cited by 31
“Indeed, it is well-documented that Tau promotes tubulin polymerization and stabilizes MTs both in vitro and in vivo (Drubin and Kirschner, 1986; Goedert and Jakes, 1990; Panda et al., 2003).”
BackgroundHuman fetal tau protein isoform: Possibilities for Alzheimer's disease treatment
Milošević, N. J., Petrović, D., Sedmak, G., Vukšić, M., Hof, P. R., & Šimić, G. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.05.001 · Cited by 34
DC11: a novel monoclonal antibody revealing Alzheimer’s disease-specific tau epitope
Vechterova, L., Kontseková, E., Žilka, N., Ferencĭk, M., Ravid, R., & Novák, M. (2003) · Neuroreport · doi:10.1097/00001756-200301200-00017 · Cited by 31
Transcellular Spreading of Tau in Tauopathies
Demaegd, K. C., Schymkowitz, J. W. H., & Rousseau, F. (2018) · ChemBioChem · doi:10.1002/cbic.201800288 · Cited by 32
Differential phosphorylation of some proteins of the neuronal cytoskeleton during brain development
Riederer, B. M. (1992) · The Histochemical Journal · doi:10.1007/bf01046350 · Cited by 31
Therapeutic Strategies for Restoring Tau HomeostasisPreprint
Young, Z. T., Mok, S., & Gestwicki, J. E. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024612 · Cited by 31
“2000) and nucleate microtubule assembly better than the 3R isoforms (Goedert and Jakes 1990).”
BackgroundInfluentialMicrotubule-associated protein tau in murine kidney: role in podocyte architecture
Vallés‐Saiz, L., Peinado-Cahuchola, R., Ávila, J., & Hernández, F. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-04106-z · Cited by 32
“Nevertheless, it should be mentioned that adult mice express mainly Tau4R isoforms in adult brain mice [42, 43] and the Tau3R isoform is expressed mainly in adult neuronal precursors [44].”
BackgroundInfluentialAggidis, A., Devitt, G., Zhang, Y., Chatterjee, S., Townsend, D. J., Fullwood, N. J., Ruiz, E., Tarutani, A., Hasegawa, M., Cooper, A. S., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14246 · Cited by 31
Hosokawa, M., Masuda‐Suzukake, M., Shitara, H., Shimozawa, A., Suzuki, G., Kondo, H., Nonaka, T., Campbell, W. D., Arai, T., & Hasegawa, M. (2021) · Brain · doi:10.1093/brain/awab289 · Cited by 30
Impaired burrowing is the most prominent behavioral deficit of aging htau mice
Geiszler, P. C., Barron, M. R., & Pardon, M. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.05.004 · Cited by 30
“In contrast, adult murine tau only consists of the 4R isoforms which do not hyperphosphorylate (Goedert and Jakes, 1990; Andorfer et al., 2003).”
Karikari, T. K., Turner, A., Stass, R., Lee, L. C. Y., Wilson, B., Nagel, D. A., Hill, E. J., & Moffat, K. G. (2016) · Protein Expression and Purification · doi:10.1016/j.pep.2016.09.009 · Cited by 31
“The resistance of tau to denaturation by SDS has been previously reported [22,23].”
BackgroundFerhat, L., Bernard, A., de Pouplana, L. R., Ben-Ari, Y., & Khrestchatisky, M. (1994) · Neurochemistry International · doi:10.1016/0197-0186(94)90139-2 · Cited by 30
MAP2d promotes bundling and stabilization of both microtubules and microfilaments
Ferhat, L., Represa, A., Bernard, A., Ben-Ari, Y., & Khrestchatisky, M. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.5.1095 · Cited by 30
KrishnaKumar, V. G., & Gupta, S. K. (2017) · Preparative Biochemistry & Biotechnology · doi:10.1080/10826068.2016.1275012 · Cited by 29
“As an alternative, recombinant tau expression for all six isoforms in Escherichia coli was reported by Goedert and Jakes,([6]) and since then bacterial expression has become a method of choice to obtain highly pure individual tau protein isoforms.”
MethodSpencer, B. J., Brüschweiler, S., Sealey‐Cardona, M., Rockenstein, E. M., Adame, A., Florio, J. B., Mante, M., Trinh, I., Rissman, R. A., Konrat, R., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1869-0 · Cited by 30
“The normal adult human brain contains approximately equal molar amounts of 3R:4RTau [28, 29, 47].”
Duquette, A., Pernègre, C., Carpentier, A. V., & Leclerc, N. M. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.607680 · Cited by 38
Giong, H.-K., Subramanian, M., Yu, K., & Lee, J.-S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168465 · Cited by 31
“In particular, the number of N is determined by alterna‐ tive splicing of exon 2 and 3 at the N terminal, whereas the number of R is defined by whether they contain repeat 2 encoded by exon 10 in mature mRNA [15,16].”
BackgroundReassessment of Neuronal Tau Distribution in Adult Human Brain and Implications for Tau Pathobiology
Paterno, G., Bell, B. M., Gorion, K.-M. M., Prokop, S., & Giasson, B. I. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01394-9 · Cited by 30
“isoforms Human tau isoforms were cloned into the pRK172 bacterial expression vector using NdeI and EcoRI restriction sites as previously described [27, 31, 75].”
Methodde Garcini, E. M., de la Luna, S., Domínguez, J. E., & Ávila, J. (1994) · Molecular and Cellular Biochemistry · doi:10.1007/bf01457399 · Cited by 29
“These tau isoforms contain three or four tubulin binding motifs, the binding to microtubules being higher in the case of those tau isoforms containing a larger number of tubulin binding motifs (Burner and Kirschner, 1991; Goedert and Jakes, 1990; Lee et al., 1989).”
BackgroundMethodModelling frontotemporal dementia using patient-derived induced pluripotent stem cells
Lines, G., Casey, J. M., Preza, E., & Wray, S. (2020) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2020.103553 · Cited by 30
“The generation of appropriate models to investigate the molecular mechanisms underpinning tauopathies such as FTD has been challenging, as immortalised cell lines and animal models do not recapitulate the complex pattern of MAPT splicing seen in the adult human CNS.”
BackgroundInfluentialMicrotubule protein phosphorylation in neuroblastoma cells and neurite growth
Díaz‐Nido, J., Armas-Portela, R., Correas, I., Domínguez, J. E., Montejo, E., & Ávila, J. (1991) · Journal of Cell Science · doi:10.1242/jcs.1991.supplement_15.8 · Cited by 29
Haque, N., Tanaka, T., Iqbal, K., & Grundke, I. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01622-4 · Cited by 29
Tau liquid–liquid phase separation: At the crossroads of tau physiology and tauopathy
Islam, M., Shen, F., Regmi, D., Petersen, K., Karim, M. R. U., & Du, D. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.30853 · Cited by 28
“0N and 1N tau isoforms make up 37% and 54% of all human brain tau, respectively, while 2N tau makes up only 9% of all tau isoforms (Goedert & Jakes, 1990; Strang et al., 2019).”
BackgroundMohammadi, Z., Alizadeh, H., Marton, J., & Cumming, P. D. (2023) · Biomolecules · doi:10.3390/biom13020290 · Cited by 28
“However, the additional repeat domain of 4R tau imparts a considerably higher affinity for microtubules in comparison with 3R tau, such that the 4R form has a more prominent role in microtubule assembly [37,39].”
BackgroundSplicing factor SC35 promotes tau expression through stabilization of its mRNA
Qian, W., Iqbal, K., Grundke, I., Gong, C., & Liu, F. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.02.017 · Cited by 28
Nuydens, R., Heers, C., Chadarevian, A., de Jong, M., Nuyens, R., Cornelissen, F. W., & Geerts, H. (1995) · Brain Research · doi:10.1016/0006-8993(95)00514-q · Cited by 28
Moraga, D., Rivas-Berrios, A., Farias, G. A., Wallin, M., & Maccioni, R. B. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90342-b · Cited by 28
Gozes, I., Iram, T., Maryanovsky, E., Arviv, C., Rozenberg, L., Schirer, Y., Giladi, E., & Furman-Assaf, S. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131664 · Cited by 27
“The microtubule associated protein tau [57, 58] displays six major isoforms in the adult human brain, all of which are derived by alternative splicing from a single gene, on the long arm of chromosome 17 [59–61].”
Cellular Biology of Tau Diversity and Pathogenic Conformers
Kang, S., Eskandari‐Sedighi, G., Hromádková, L., Safar, J., & Westaway, D. A. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590199 · Cited by 29
The Power and Richness of Modelling Tauopathies in Drosophila
Papanikolopoulou, K., & Skoulakis, E. M. C. (2011) · Molecular Neurobiology · doi:10.1007/s12035-011-8193-1 · Cited by 29
“In normal adult human tissue, the ratio of 4R/3R Tau is ∼1 [32, 33].”
BackgroundStudying tauopathies in Drosophila: A fruitful model
Sun, M., & Chen, L. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.03.029 · Cited by 27
Phosphorylation of human microtubule‐associated protein tau by protein kinases of the AGC subfamily
Virdee, K., Yoshida, H., Peak‐Chew, S., & Goedert, M. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.05.009 · Cited by 27
“coli from cDNA clone htau46 and expressed as described [33].”
MethodSelf-citationNeurotoxic dopamine quinone facilitates the assembly of tau into fibrillar polymers
Santa‐María, I., Hernández, F., Smith, M. A., Perry, G. L., Ávila, J., & Moreno, F. J. (2005) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-005-7499-6 · Cited by 27
“Briefly, htau 42 was cloned into vector pRK172 [22] for inducible expression in E.”
MethodLo, M., Fieles, A., Norris, T., Dargis, P., Caputo, C., Scott, C. W., Lee, V. M.-Y., & Goedert, M. (1993) · Brain Research. Molecular Brain Research · doi:10.1016/0169-328x(93)90043-o · Cited by 27
Self-citationEllis, M. J., Lekka, C., Holden, K. L., Tulmin, H., Seedat, F., O'Brien, D. P., Dhayal, S., Zeissler, M., Knudsen, J. G., Kessler, B. M., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02729-7 · Cited by 26
“…predicted molecular weights (MW) ranging from 36.7 to 45.9 kDa, but migrate on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) as a series of closely spaced bands with apparent MWs ranging from 58 to 66 kDa, thus showing abnormal retardation in electrophoretic mobility [64].”
Influential
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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