The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
The Endogenous and Cell Cycle-dependent Phosphorylation of tau Protein in Living Cells: Implications for Alzheimer’s Disease
Open accessAbstract
In Alzheimer’s disease the neuronal microtubule-associated protein tau becomes highly phosphorylated, loses its binding properties, and aggregates into paired helical filaments. There is increasing evidence that the events leading to this hyperphosphorylation are related to mitotic mechanisms. Hence, we have analyzed the physiological phosphorylation of endogenous tau protein in metabolically labeled human neuroblastoma cells and in Chinese hamster ovary cells stably transfected with tau. In nonsynchronized cultures the phosphorylation pattern was remarkably similar in both cell lines, suggesting a similar balance of kinases and phosphatases with respect to tau. Using phosphopeptide mapping and sequencing we identified 17 phosphorylation sites comprising 80–90% of the total phosphate incorporated. Most of these are in SP or TP motifs, except S214 and S262. Since phosphorylation of microtubule-associated proteins increases during mitosis, concomitant with increased microtubule dynamics, we analyzed cells mitotically arrested with nocodazole. This revealed that S214 is a prominent phosphorylation site in metaphase, but not in interphase. Phosphorylation of this residue strongly decreases the tau–microtubule interaction in vitro, suppresses microtubule assembly, and may be a key factor in the observed detachment of tau from microtubules during mitosis. Since S214 is also phosphorylated in Alzheimer’s disease tau, our results support the view that reactivation of the cell cycle machinery is involved in tau hyperphosphorylation.
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Cites
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
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Domains of tau Protein and Interactions with Microtubules
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Self-citationMonoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
Goedert, M., Jakes, R., & Vanmechelen, E. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)11484-e · Cited by 608
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Monoclonal antibody PHF‐1 recognizes tau protein phosphorylated at serine residues 396 and 404
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“Among the identified phosphopeptides, only four (T181, S202/T205*, T231/S235, and S396/S404) would be detected immunocytochemically with the monoclonal antibodies AT270, AT8, AT180, and PHF-1, respectively (Biernat et al., 1992; Goedert et al., 1995).”
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Cited by
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
Augustinack, J. C., Schneider, A., Mandelkow, E.-M., & Hyman, B. T. (2002) · Acta Neuropathologica · doi:10.1007/s004010100423 · Cited by 998
Self-citationBiochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration
Mandelkow, E.-M., & Mandelkow, E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006247 · Cited by 847
Self-citationEbneth, A., Godemann, R., Stamer, K., Illenberger, S., Trinczek, B., Mandelkow, E.-M., & Mandelkow, E. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.3.777 · Cited by 820
Self-citationThe prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
Lu, P.-J., Wulf, G., Zhou, X. Z., Davies, P., & Lu, K. P. (1999) · Nature · doi:10.1038/21650 · Cited by 721
Metadata
- Authors
- Illenberger, S., Zheng-Fischhöfer, Q., Preuss, U., Stamer, K., Baumann, K., Trinczek, B., Biernat, J., Godemann, R., Mandelkow, E.-M., & Mandelkow, E.
- Venue
- Molecular Biology of the Cell
- Published
- 1998-06
- Volume
- 9
- Issue
- 6
- Pages
- 1495-1512
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2114302599
- Cited by
- 304
- References
- 12
- FWCI
- 9.64
- Type
- journal article
- Language
- en
- Open access
- green
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- Illenberger, S., Zheng-Fischhöfer, Q., Preuss, U., Stamer, K., Baumann, K., Trinczek, B., Biernat, J., Godemann, R., Mandelkow, E.-M., & Mandelkow, E. (1998). The Endogenous and Cell Cycle-dependent Phosphorylation of tau Protein in Living Cells: Implications for Alzheimer’s Disease. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.9.6.1495
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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