Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 11 November 1988:
Vol. 242. no. 4880, pp. 936 - 939
DOI: 10.1126/science.3142041
Prev | Table of Contents | Next

Articles

Science, Vol 242, Issue 4880, 936-939
Copyright © 1988 by American Association for the Advancement of Science

articles

Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein

SA Lewis, DH Wang, and NJ Cowan

Department of Biochemistry, New York University Medical Center, NY 10016.

The microtubule-associated protein MAP2 is a prominent large-sized component of purified brain microtubules that, like the 36- to 38-kilodalton tau proteins, bears antigenic determinants found in association with the neurofibrillary tangles of Alzheimer's disease. The complete sequence of mouse brain MAP2 was determined from a series of overlapping cloned complementary DNAs. The sequence of the carboxyl-terminal 185 amino acids is very similar (67 percent) to a corresponding region of tau protein, and includes a series of three imperfect repeats, each 18 amino acids long and separated by 13 or 14 amino acids. A subcloned fragment spanning the first two of the 18-amino acid repeats was expressed as a polypeptide by translation in vitro. This polypeptide copurified with microtubules through two successive cycles of polymerization and depolymerization, whereas a control polypeptide derived from the amino-terminal region of MAP2 completely failed to copurify. These data imply that the carboxyl-terminal domain containing the 18-amino acid repeats constitutes the microtubule binding site in MAP2. The occurrence of these repeats in tau protein suggests that these may be a general feature of microtubule binding proteins.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Conformational Diversity of Wild-type Tau Fibrils Specified by Templated Conformation Change.
B. Frost, J. Ollesch, H. Wille, and M. I. Diamond (2009)
J. Biol. Chem. 284, 3546-3551
   Abstract »    Full Text »    PDF »
Mtap2 Is a Constituent of the Protein Network That Regulates Twik-Related K+ Channel Expression and Trafficking.
G. Sandoz, M. P. Tardy, S. Thummler, S. Feliciangeli, M. Lazdunski, and F. Lesage (2008)
J. Neurosci. 28, 8545-8552
   Abstract »    Full Text »    PDF »
Association of Tyrosine Phosphatase Epsilon with Microtubules Inhibits Phosphatase Activity and Is Regulated by the Epidermal Growth Factor Receptor.
T. Sines, S. Granot-Attas, S. Weisman-Welcher, and A. Elson (2007)
Mol. Cell. Biol. 27, 7102-7112
   Abstract »    Full Text »    PDF »
p180 Is Involved in the Interaction between the Endoplasmic Reticulum and Microtubules through a Novel Microtubule-binding and Bundling Domain.
K. Ogawa-Goto, K. Tanaka, T. Ueno, K. Tanaka, T. Kurata, T. Sata, and S. Irie (2007)
Mol. Biol. Cell 18, 3741-3751
   Abstract »    Full Text »    PDF »
Association of Ebola Virus Matrix Protein VP40 with Microtubules.
G. Ruthel, G. L. Demmin, G. Kallstrom, M. P. Javid, S. S. Badie, A. B. Will, T. Nelle, R. Schokman, T. L. Nguyen, J. H. Carra, et al. (2005)
J. Virol. 79, 4709-4719
   Abstract »    Full Text »    PDF »
A comparison of the ability of XMAP215 and tau to inhibit the microtubule destabilizing activity of XKCM1.
T. L Noetzel, D. N Drechsel, A. A Hyman, and K. Kinoshita (2005)
Phil Trans R Soc B 360, 591-594
   Abstract »    Full Text »    PDF »
Cysteine Oxidation of Tau and Microtubule-associated Protein-2 by Peroxynitrite: MODULATION OF MICROTUBULE ASSEMBLY KINETICS BY THE THIOREDOXIN REDUCTASE SYSTEM.
L. M. Landino, T. E. Skreslet, and J. A. Alston (2004)
J. Biol. Chem. 279, 35101-35105
   Abstract »    Full Text »    PDF »
Characterization of Functional Domains of Human EB1 Family Proteins.
W. Bu and L.-K. Su (2003)
J. Biol. Chem. 278, 49721-49731
   Abstract »    Full Text »    PDF »
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)
J. Biol. Chem. 278, 29609-29618
   Abstract »    Full Text »    PDF »
In Vitro Assembly of Alzheimer-like Filaments. HOW A SMALL CLUSTER OF CHARGED RESIDUES IN Tau AND MAP2 CONTROLS FILAMENT MORPHOLOGY.
M. A. DeTure, L. Di Noto, and D. L. Purich (2002)
J. Biol. Chem. 277, 34755-34759
   Abstract »    Full Text »    PDF »
MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments.
J. Al-Bassam, R. S. Ozer, D. Safer, S. Halpain, and R. A. Milligan (2002)
J. Cell Biol. 157, 1187-1196
   Abstract »    Full Text »    PDF »
A novel polymer of tubulin forms the conoid of Toxoplasma gondii.
K. Hu, D. S. Roos, and J. M. Murray (2002)
J. Cell Biol. 156, 1039-1050
   Abstract »    Full Text »    PDF »
Direct binding of NuMA to tubulin is mediated by a novel sequence motif in the tail domain that bundles and stabilizes microtubules.
L. Haren and A. Merdes (2002)
J. Cell Sci. 115, 1815-1824
   Abstract »    Full Text »    PDF »
Phosphorylation-dependent Localization of Microtubule-associated Protein MAP2c to the Actin Cytoskeleton.
R. S. Ozer and S. Halpain (2000)
Mol. Biol. Cell 11, 3573-3587
   Abstract »    Full Text »
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
   Abstract »    Full Text »    PDF »
Functional Elements within the Dynein Microtubule-binding Domain.
M. P. Koonce and I. Tikhonenko (2000)
Mol. Biol. Cell 11, 523-529
   Abstract »    Full Text »
A Nonerythroid Isoform of Protein 4.1R Interacts with the Nuclear Mitotic Apparatus (NuMA) Protein.
S. N. Mattagajasingh, S.-C. Huang, J. S. Hartenstein, M. Snyder, V. T. Marchesi, and E. J. Benz Jr. (1999)
J. Cell Biol. 145, 29-43
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
Herpes Simplex Virus Type 1 Tegument Protein VP22 Induces the Stabilization and Hyperacetylation of Microtubules.
G. Elliott and P. O'Hare (1998)
J. Virol. 72, 6448-6455
   Abstract »    Full Text »    PDF »
Purification of a WD Repeat Protein, EMAP, That Promotes Microtubule Dynamics through an Inhibition of Rescue.
D. R. Hamill, B. Howell, L. Cassimeris, and K. A. Suprenant (1998)
J. Biol. Chem. 273, 9285-9291
   Abstract »    Full Text »    PDF »
Stu2p: A Microtubule-Binding Protein that Is an Essential Component of the Yeast Spindle Pole Body.
P. J. Wang and T. C. Huffaker (1997)
J. Cell Biol. 139, 1271-1280
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
The Neurofibrillary Pathology of Alzheimer's Disease.
M. Goedert (1997)
Neuroscientist 3, 131-141
   Abstract »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    PDF »
Emergence of Activity-Dependent, Bidirectional Control of Microtubule-Associated Protein MAP2 Phosphorylation during Postnatal Development.
E. M. Quinlan and S. Halpain (1996)
J. Neurosci. 16, 7627-7637
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
Cloning and Characterization of a Novel A-kinase Anchoring Protein.
L. B. Lester, V. M. Coghlan, B. Nauert, and J. D. Scott (1996)
J. Biol. Chem. 271, 9460-9465
   Abstract »    Full Text »    PDF »
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 »
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 »
The C Terminus of Mitosin Is Essential for Its Nuclear Localization, Centromere/Kinetochore Targeting, and Dimerization.
X. Zhu, K.-H. Chang, D. He, M. A. Mancini, W. R. Brinkley, and W.-H. Lee (1995)
J. Biol. Chem. 270, 19545-19550
   Abstract »    Full Text »    PDF »
Non-cooperative Binding of the MAP-2 Microtubule-binding Region to Microtubules.
R. L. Coffey and D. L. Purich (1995)
J. Biol. Chem. 270, 1035-1040
   Abstract »    Full Text »    PDF »
Mitotic regulation of microtubule cross-linking activity of CENP-E kinetochore protein.
H Liao, G Li, and T. Yen (1994)
Science 265, 394-398
   Abstract »    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 »
A tau-like protein interacts with stress fibers and microtubules in human and rodent cultured cell lines.
D Cross, C Vial, and R. Maccioni (1993)
J. Cell Sci. 105, 51-60
   Abstract »    PDF »
Nuclear proteins of the bovine esophageal epithelium. II. The NuMA gene gives rise to multiple mRNAs and gene products reactive with monoclonal antibody W1.
T. Tang, C. Tang, Y. Chen, and C. Wu (1993)
J. Cell Sci. 104, 249-260
   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 »
Brain microtubule-associated proteins modulate microtubule dynamic instability in vitro. Real-time observations using video microscopy.
N. K. Pryer, R. A. Walker, V. P. Skeen, B. D. Bourns, M. F. Soboeiro, and E. D. Salmon (1992)
J. Cell Sci. 103, 965-976
   Abstract »    PDF »
Reorganisation of the microtubular cytoskeleton by embryonic microtubule-associated protein 2 (MAP2c).
B. Weisshaar, T. Doll, and A. Matus (1992)
Development 116, 1151-1161
   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 »
Regulated Association of Microtubule-associated Protein 2 (MAP2) with Src and Grb2: Evidence for MAP2 as a Scaffolding Protein.
R. W. L. Lim and S. Halpain (2000)
J. Biol. Chem. 275, 20578-20587
   Abstract »    Full Text »    PDF »
Differential Binding Regulation of Microtubule-associated Proteins MAP1A, MAP1B, and MAP2 by Tubulin Polyglutamylation.
C. Bonnet, D. Boucher, S. Lazereg, B. Pedrotti, K. Islam, P. Denoulet, and J. C. Larcher (2001)
J. Biol. Chem. 276, 12839-12848
   Abstract »    Full Text »    PDF »
Functional Differences of Tau Isoforms Containing 3 or 4 C-terminal Repeat Regions and the Influence of Oxidative Stress.
M. A. Utton, G. M. Gibb, I. D. J. Burdett, B. H. Anderton, and A. Vandecandelaere (2001)
J. Biol. Chem. 276, 34288-34297
   Abstract »    Full Text »    PDF »
Identification of Novel Bifunctional Calmodulin-binding and Microtubule-stabilizing Motifs in STOP Proteins.
C. Bosc, R. Frank, E. Denarier, M. Ronjat, A. Schweitzer, J. Wehland, and D. Job (2001)
J. Biol. Chem. 276, 30904-30913
   Abstract »    Full Text »    PDF »
The Human EMAP-like Protein-70 (ELP70) Is a Microtubule Destabilizer That Localizes to the Mitotic Apparatus.
B. Eichenmuller, P. Everley, J. Palange, D. Lepley, and K. A. Suprenant (2002)
J. Biol. Chem. 277, 1301-1309
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)