Abstract
Tau is one of the diverse group of microtubule-associated proteins that bind to microtubules and may thereby influence their structure and function. It occurs in the mammalian brain1, mainly in axons, and is a component of the neurofibrillary tangles of Alzheimer's disease2,3. Tau was recently sequenced4, but there remains a shortage of structural data on the protein. We have now prepared paracrystals of tau suitable for electron microscopy and image processing. They show distinct transverse banding and polarity, indicating that the protein subunits are aligned with the same orientations. In contrast to other paracrystals, those of tau protein can stretch or contract continuously by more than three-fold; the axial repeats range from 22 to 68 nm. After scaling to a common period, the density distributions are closely superimposable. This suggests that tau is an elastic molecule.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Weingarten, M. D., Lockwood, A. H., Hwo, S. Y. & Kirschner, M. W. Proc. natn. Acad. Sci. U.S.A. 72, 1858–1862 (1975).
Kosik, K., Joachim, C. & Selkoe, D. Proc. natn. Acad. Sci U.S.A. 83, 4044–4048 (1986).
Wood, J., Mirra, S., Pollock, N. & Binder, L. Proc. natn. Acad. Sci. U.S.A. 83, 4040–4043 (1986).
Lee, G., Cowan, N. & Kirschner, M. Science 239, 285–288 (1988).
Fellous, A., Francon, J., Lennon, A. M. & Nunez, J. Eur. J. Biochem. 78, 167–174 (1977).
Lindwall, G. & Cole, R. D. J. biol. Chem. 259, 12241–12245 (1984).
Doyle, B., Hukins, D., Hulmes, D., Miller, A. & Woodhead-Galloway, J. J. molec. Biol. 91, 79–99 (1975).
Caspar, D. L. D., Cohen, C. & Longley, W. J. molec. Biol 41, 87–107 (1969).
Cleveland, D. W., Hwo, S.-Y. & Kirschner, M. W. J. molec. Biol. 116, 227–247 (1977).
Raju, K. & Anwar, R. A. J. biol. Chem. 262, 5755–5762 (1987).
Weis-Fogh, T. & Andersen, S. O. Nature 227, 718–721 (1970).
Allen, R. D. et al. J. Cell Biol. 100, 1736–1752 (1985).
Mandelkow, E.-M., Herrmann, M. & Rühl, U. J. molec. Biol. 185, 311–327 (1985).
Van Bruggen, E., van Breemen, J., Keegstra, W., Boekema, E. & van Heel, M. J. Microsc. 141, 11–20 (1986).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Lichtenberg, B., Mandelkow, EM., Hagestedt, T. et al. Structure and elasticity of microtubule-associated protein tau. Nature 334, 359–362 (1988). https://doi.org/10.1038/334359a0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/334359a0
This article is cited by
-
O-GlcNAcylation as a Therapeutic Target for Alzheimer’s Disease
NeuroMolecular Medicine (2020)
-
Application of multilayered strategy for variable selection in QSAR modeling of PET and SPECT imaging agents as diagnostic agents for Alzheimer’s disease
Structural Chemistry (2019)
-
Transgenic animal models of Alzheimer's disease and related disorders: histopathology, behavior and therapy
Molecular Psychiatry (2004)
-
Tau as a nucleolar protein in human nonneural cells in vitro and in vivo
Chromosoma (1996)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.
