The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain.
Open accessAbstract
The neuronal microtubule-associated protein tau is required for the development of cell polarity in cultured neurons. Using PC12 cells that stably express tau and tau amino-terminal fragments, we report that tau interacts with the neural plasma membrane through its amino-terminal projection domain. In differentiated PC12 transfectants, tau is found in growth cone-like structures in a nonmicrotubule-dependent manner. In hippocampal neurons, tau is differentially extracted by detergent and enriched in the growth cone and the distal axon when membrane is left intact. In PC12 transfectants, overexpression of tau's amino-terminal fragment, but not of full-length tau, suppresses NGF-induced process formation. Our data suggest that tau's amino-terminal projection domain has an important role in neuritic development and establishes tau as a mediator of microtubule-plasma membrane interactions.
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Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
The establishment of polarity by hippocampal neurons in culture.
Dotti, C., Sullivan, C., & Banker, G. (1988) · The Journal of Neuroscience · doi:10.1523/jneurosci.08-04-01454.1988 · Cited by 1,862
Domains of tau Protein and Interactions with Microtubules
Gustke, N., Trinczek, B., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1994) · Biochemistry · doi:10.1021/bi00198a017 · Cited by 655
Phosphorylation determines two distinct species of tau in the central nervous system
Papasozomenos, S. C., & Binder, L. I. (1987) · Cell Motility · doi:10.1002/cm.970080303 · Cited by 420
Goode, B., & Feinstein, S. (1994) · The Journal of cell biology · doi:10.1083/jcb.124.5.769 · Cited by 399
Phosphorylation 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
Kanai, Y., & Hirokawa, N. (1995) · Neuron · doi:10.1016/0896-6273(95)90298-8 · Cited by 144 · cited 1×
“Kanai and Hirokawa (1995) have suggested that the localization of tau to the axon is based on the microtubule binding properties of the carboxy terminal half of tau.”
Cited by
Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174
Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003
Role of tau protein in both physiological and pathological conditions
AVILA, J., LUCAS, J. J., PÉREZ, M., & HERNÁNDEZ, F. (2004) · Physiological Reviews · doi:10.1152/physrev.00024.2003 · Cited by 1,005
Mandelkow, E. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01368-3 · Cited by 953
Morris, M., Maeda, S., Vossel, K., & Mucke, L. (2011) · Neuron · doi:10.1016/j.neuron.2011.04.009 · Cited by 899
Metadata
- Authors
- Brandt, R., Léger, J., & Lee, G.
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1995-12-01
- Volume
- 131
- Issue
- 5
- Pages
- 1327-1340
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W1971125966
- Cited by
- 625
- References
- 7
- FWCI
- 7.18
- Type
- journal article
- Language
- en
- Open access
- green
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