The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Tau protein function in living cells.
Abstract
Tau protein from mammalian brain promotes microtubule polymerization in vitro and is induced during nerve cell differentiation. However, the effects of tau or any other microtubule-associated protein on tubulin assembly within cells are presently unknown. We have tested tau protein activity in vivo by microinjection into a cell type that has no endogenous tau protein. Immunofluorescence shows that tau protein microinjected into fibroblast cells associates specifically with microtubules. The injected tau protein increases tubulin polymerization and stabilizes microtubules against depolymerization. This increased polymerization does not, however, cause major changes in cell morphology or microtubule arrangement. Thus, tau protein acts in vivo primarily to induce tubulin assembly and stabilize microtubules, activities that may be necessary, but not sufficient, for neuronal morphogenesis.
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“The protein Tau aggregates into tangles in the brain of patients with Alzheimer’s disease.”
From Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau (2017) · cites this paper as [2]
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Citations
Cites
Dynamic instability of microtubule growth
Mitchison, T., & Kirschner, M. (1984) · Nature · doi:10.1038/312237a0 · Cited by 3,337
Self-citationCleveland, D. W., Hwo, S.-Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90213-3 · Cited by 915 · cited 2×
“These include the tau proteins of 50-70 kD (Weingarten et al., 1975; Cleveland et al., 1977), microtubule-associated protein 1 (MAP1) ~ of '~330 kD, and microtubule-associated protein 2 (MAP2) of "~300 kD (for a review of MAP1 and MAP2 see Vallee et al., 1984).”
Self-citationPhosphorylation of microtubule-associated proteins regulates their interaction with actin filaments.
Selden, S. C., & Pollard, T. D. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32333-0 · Cited by 314
Cited by
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
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
Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., & Lee, V. M. Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90057-x · Cited by 903
Stamer, K., Vogel, R., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108057 · Cited by 885
Tau and neurodegenerative disease: the story so far
Iqbal, K., Liu, F., & Gong, C.-X. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.225 · Cited by 806
Metadata
- Authors
- Drubin, D. G., & Kirschner, M. W.
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1986-12-01
- Volume
- 103
- Issue
- 6
- Pages
- 2739-2746
- ISSN
- 0021-9525
- 1540-8140
- PMC
- PMC2114585
- Cited by
- 652
- References
- 3
- Language
- en
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