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Science 15 January 1988:
Vol. 239. no. 4837, pp. 285 - 288
DOI: 10.1126/science.3122323
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Articles

Science, Vol 239, Issue 4837, 285-288
Copyright © 1988 by American Association for the Advancement of Science

articles

The primary structure and heterogeneity of tau protein from mouse brain

G Lee, N Cowan, and M Kirschner

Department of Neurology, Harvard Medical School, Boston, MA 02115.

Tau protein is a family of microtubule binding proteins, heterogeneous in molecular weight, that are induced during neurite outgrowth and are found prominently in neurofibrillary tangles in Alzheimer's disease. The predicted amino acid sequences of two forms of tau protein from mouse brain were determined from complementary DNA clones. These forms are identical in their amino-terminal sequences but differ in their carboxyl-terminal domains. Both proteins contain repeated sequences that may be tubulin binding sites. The sequence suggests that tau is an elongated molecule with no extensive alpha-helical or beta-sheet domains. These complementary DNAs should enable the study of various functional domains of tau and the study of tau expression in normal and pathological states.


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Proline-directed Pseudo-phosphorylation at AT8 and PHF1 Epitopes Induces a Compaction of the Paperclip Folding of Tau and Generates a Pathological (MC-1) Conformation.
S. Jeganathan, A. Hascher, S. Chinnathambi, J. Biernat, E.-M. Mandelkow, and E. Mandelkow (2008)
J. Biol. Chem. 283, 32066-32076
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K. J. Rosenberg, J. L. Ross, H. E. Feinstein, S. C. Feinstein, and J. Israelachvili (2008)
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A Cell Number-Counting Factor Regulates Levels of a Novel Protein, SslA, as Part of a Group Size Regulation Mechanism in Dictyostelium.
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The "Jaws" of the Tau-Microtubule Interaction.
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FTDP-17 Mutations Compromise the Ability of Tau to Regulate Microtubule Dynamics in Cells.
J. M. Bunker, K. Kamath, L. Wilson, M. A. Jordan, and S. C. Feinstein (2006)
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Possible Role of Each Repeat Structure of the Microtubule-Binding Domain of the Tau Protein in In Vitro Aggregation.
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Cell-Cycle Reentry and Cell Death in Transgenic Mice Expressing Nonmutant Human Tau Isoforms.
C. Andorfer, C. M. Acker, Y. Kress, P. R. Hof, K. Duff, and P. Davies (2005)
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The Invs Gene Encodes a Microtubule-Associated Protein.
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J. Am. Soc. Nephrol. 15, 1700-1710
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Modulation of Microtubule Dynamics by Tau in Living Cells: Implications for Development and Neurodegeneration.
J. M. Bunker, L. Wilson, M. A. Jordan, and S. C. Feinstein (2004)
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The Abl-related gene (Arg) requires its F-actin-microtubule cross-linking activity to regulate lamellipodial dynamics during fibroblast adhesion.
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Role of Tau Protein in Both Physiological and Pathological Conditions.
J. AVILA, J. J. LUCAS, M. PEREZ, and F. HERNANDEZ (2004)
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The Number of Repeat Sequences in Microtubule-associated Protein 4 Affects the Microtubule Surface Properties.
K. Tokuraku, K. Matsushima, T. Matui, H. Nakagawa, M. Katsuki, R. Majima, and S. Kotani (2003)
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Glycogen Synthase Kinase 3beta Phosphorylates Tau at Both Primed and Unprimed Sites. DIFFERENTIAL IMPACT ON MICROTUBULE BINDING.
J.-H. Cho and G. V. W. Johnson (2003)
J. Biol. Chem. 278, 187-193
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Protein Kinase MARK/PAR-1 Is Required for Neurite Outgrowth and Establishment of Neuronal Polarity.
J. Biernat, Y.-Z. Wu, T. Timm, Q. Zheng-Fischhofer, E. Mandelkow, L. Meijer, and E.-M. Mandelkow (2002)
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Structure, Stability, and Aggregation of Paired Helical Filaments from Tau Protein and FTDP-17 Mutants Probed by Tryptophan Scanning Mutagenesis.
L. Li, M. von Bergen, E.-M. Mandelkow, and E. Mandelkow (2002)
J. Biol. Chem. 277, 41390-41400
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The Novel Adaptor Protein, Mti1p, and Vrp1p, a Homolog of Wiskott-Aldrich Syndrome Protein-Interacting Protein (WIP), May Antagonistically Regulate Type I Myosins in Saccharomyces cerevisiae.
J. Mochida, T. Yamamoto, K. Fujimura-Kamada, and K. Tanaka (2002)
Genetics 160, 923-934
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Mutations of Tau Protein in Frontotemporal Dementia Promote Aggregation of Paired Helical Filaments by Enhancing Local beta -Structure.
M. von Bergen, S. Barghorn, L. Li, A. Marx, J. Biernat, E.-M. Mandelkow, and E. Mandelkow (2001)
J. Biol. Chem. 276, 48165-48174
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Diversity and phylogeny of gephyrin: Tissue-specific splice variants, gene structure, and sequence similarities to molybdenum cofactor-synthesizing and cytoskeleton-associated proteins.
M. Ramming, S. Kins, N. Werner, A. Hermann, H. Betz, and J. Kirsch (2000)
PNAS 97, 10266-10271
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The Microtubule Binding of Tau and High Molecular Weight Tau in Apoptotic PC12 Cells Is Impaired because of Altered Phosphorylation.
P. K. Davis and G. V. W. Johnson (1999)
J. Biol. Chem. 274, 35686-35692
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Phosphorylated tau can promote tubulin assembly.
H.-C. Tseng, Q. Lu, E. Henderson, and D. J. Graves (1999)
PNAS 96, 9503-9508
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Dynamic Regulation of Expression and Phosphorylation of Tau by Fibroblast Growth Factor-2 In Neural Progenitor Cells from Adult Rat Hippocampus.
Y. Tatebayashi, K. Iqbal, and I. Grundke-Iqbal (1999)
J. Neurosci. 19, 5245-5254
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GMAP-210, A Cis-Golgi Network-associated Protein, Is a Minus End Microtubule-binding Protein.
C. Infante, F. Ramos-Morales, C. Fedriani, M. Bornens, and R. M. Rios (1999)
J. Cell Biol. 145, 83-98
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The Development of Cell Processes Induced by tau Protein Requires Phosphorylation of Serine 262 and 356 in the Repeat Domain and Is Inhibited by Phosphorylation in the Proline-rich Domains.
J. Biernat and E.-M. Mandelkow (1999)
Mol. Biol. Cell 10, 727-740
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Transgenic Expression of the Shortest Human Tau Affects Its Compartmentalization and Its Phosphorylation as in the Pretangle Stage of Alzheimer's Disease.
J.-P. Brion, G. Tremp, and J.-N. Octave (1999)
Am. J. Pathol. 154, 255-270
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A nucleated assembly mechanism of Alzheimer paired helical filaments.
P. Friedhoff, M. von Bergen, E.-M. Mandelkow, P. Davies, and E. Mandelkow (1998)
PNAS 95, 15712-15717
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The Endogenous and Cell Cycle-dependent Phosphorylation of tau Protein in Living Cells: Implications for Alzheimer's Disease.
S. Illenberger, Q. Zheng-Fischhöfer, U. Preuss, K. Stamer, K. Baumann, B. Trinczek, J. Biernat, R. Godemann, E.-M. Mandelkow, and E. Mandelkow (1998)
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Expression of specific tau exons in normal and tumoral pancreatic acinar cells.
M. Vanier, P Neuville, L Michalik, and J. Launay (1998)
J. Cell Sci. 111, 1419-1432
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Stu2p: A Microtubule-Binding Protein that Is an Essential Component of the Yeast Spindle Pole Body.
P. J. Wang and T. C. Huffaker (1997)
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Domains of Neuronal Microtubule-associated Proteins and Flexural Rigidity of Microtubules.
H. Felgner, R. Frank, J. Biernat, E.-M. Mandelkow, E. Mandelkow, B. Ludin, A. Matus, and M. Schliwa (1997)
J. Cell Biol. 138, 1067-1075
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The Neurofibrillary Pathology of Alzheimer's Disease.
M. Goedert (1997)
Neuroscientist 3, 131-141
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Molecular Characterization of p62, a Mitotic Apparatus Protein Required for Mitotic Progression.
X. Ye and R. D. Sloboda (1997)
J. Biol. Chem. 272, 3606-3614
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The 'jaws' model of tau-microtubule interaction examined in CHO cells.
U Preuss, J Biernat, E. Mandelkow, and E Mandelkow (1997)
J. Cell Sci. 110, 789-800
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Phosphorylation of Microtubule-associated Proteins MAP2 and MAP4 by the Protein Kinase p110[IMAGE].
S. Illenberger, G. Drewes, B. Trinczek, J. Biernat, H. E. Meyer, J. B. Olmsted, E.-M. Mandelkow, and E. Mandelkow (1996)
J. Biol. Chem. 271, 10834-10843
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PTL-1, a microtubule-associated protein with tau-like repeats from the nematode Caenorhabditis elegans.
M Goedert, C. Baur, J Ahringer, R Jakes, M Hasegawa, M. Spillantini, M. Smith, and F Hill (1996)
J. Cell Sci. 109, 2661-2672
   Abstract »    PDF »
Blackjack, a novel protein associated with microtubules in embryonic neurons.
K. Zachow and D Bentley (1996)
J. Cell Sci. 109, 1497-1507
   Abstract »    PDF »
A muscle-specific variant of microtubule-associated protein 4 (MAP4) is required in myogenesis.
M. Mangan and J. Olmsted (1996)
Development 122, 771-781
   Abstract »    PDF »
Molecular Dissection of the Neurofibrillary Lesions of Alzheimer's Disease.
M. Goedert, M.G. Spillantini, M. Hasegawa, R. Jakes, R.A. Crowther, and A. Klug (1996)
Cold Spring Harb Symp Quant Biol 61, 565-573
   Abstract »    PDF »
Puromycin-sensitive Aminopeptidase.
D. B. Constam, A. R. Tobler, A. Rensing-Ehl, I. Kemler, L. B. Hersh, and A. Fontana (1995)
J. Biol. Chem. 270, 26931-26939
   Abstract »    Full Text »    PDF »
Sequence analysis of MAP2 function in living cells.
J Ferralli, T Doll, and A Matus (1994)
J. Cell Sci. 107, 3115-3125
   Abstract »    PDF »
Identification of a novel microtubule-binding domain in microtubule-associated protein 1A (MAP1A).
A Cravchik, D Reddy, and A Matus (1994)
J. Cell Sci. 107, 661-672
   Abstract »    PDF »
Kinesin and tau bind to distinct sites on microtubules.
P. Marya, Z Syed, P. Fraylich, and P. Eagles (1994)
J. Cell Sci. 107, 339-344
   Abstract »    PDF »
An isoform of microtubule-associated protein 2 (MAP2) containing four repeats of the tubulin-binding motif.
T Doll, M Meichsner, B. Riederer, P Honegger, and A Matus (1993)
J. Cell Sci. 106, 633-639
   Abstract »    PDF »
Expression of high molecular weight tau in the central and peripheral nervous systems.
I. Georgieff, R. Liem, D Couchie, C Mavilia, J Nunez, and M. Shelanski (1993)
J. Cell Sci. 105, 729-737
   Abstract »    PDF »
Primary structure and microtubule-interacting domain of the SP-H antigen: a mitotic MAP located at the spindle pole and characterized as a homologous protein to NuMA.
T Maekawa and R Kuriyama (1993)
J. Cell Sci. 105, 589-600
   Abstract »    PDF »
Actin depolymerisation induces process formation on MAP2-transfected non-neuronal cells.
K Edson, B Weisshaar, and A Matus (1993)
Development 117, 689-700
   Abstract »    PDF »
Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau.
R. Takemura, S. Okabe, T. Umeyama, Y. Kanai, N. J. Cowan, and N. Hirokawa (1992)
J. Cell Sci. 103, 953-964
   Abstract »    PDF »
Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E.
C Wilson, M. Wardell, K. Weisgraber, R. Mahley, and D. Agard (1991)
Science 252, 1817-1822
   Abstract »    PDF »
Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein.
S. Lewis, D. Wang, and N. Cowan (1988)
Science 242, 936-939
   Abstract »    PDF »
Large microtubule-associated protein of T. brucei has tandemly repeated, near-identical sequences.
A Schneider, A Hemphill, T Wyler, and T Seebeck (1988)
Science 241, 459-462
   Abstract »    PDF »
Structural and Functional Differences between 3-Repeat and 4-Repeat Tau Isoforms. IMPLICATIONS FOR NORMAL TAU FUNCTION AND THE ONSET OF NEURODEGENERATIVE DISEASE.
B. L. Goode, M. Chau, P. E. Denis, and S. C. Feinstein (2000)
J. Biol. Chem. 275, 38182-38189
   Abstract »    Full Text »    PDF »


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