Cell type-specific processing of human Tau proteins in Drosophila
Open accessAbstract
Accumulation of hyperphosphorylated Tau is associated with a number of neurodegenerative diseases collectively known as tauopathies. Differences in clinical and cognitive profiles among them suggest differential sensitivity of neuronal populations to Tau levels, phosphorylation and mutations. We used tissue specific expression of wild type and mutant human tau transgenes to demonstrate differential phosphorylation and stability in a cell type‐specific manner, which includes different neuronal types and does not correlate with the level of accumulated protein. Rather, they likely reflect the spatial distribution or regulation of Tau‐targeting kinases and phosphatases.
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Drosophila models expressing human tau recapitulate key features of human tauopathies, including progressive neurodegeneration and phosphorylation at AD-related sites via conserved kinases.
“Drosophila models expressing human tau recapitulate key features of human tauopathies, including progressive neurodegeneration and phosphorylation at AD-related sites via conserved kinases [41, 44, 53, 59–63].”
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GSK-3β inhibition reverses axonal transport defects and behavioural phenotypes in Drosophila
Mudher, A., Shepherd, D., Newman, T. A., Mildren, P., Jukes, J. P., Squire, A., Mears, A., Berg, S., MacKay, D., Asuni, A. A., et al. (2004) · Molecular Psychiatry · doi:10.1038/sj.mp.4001483 · Cited by 265 · see citing works
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- Yeh, E., Gustafson, K. and Boulianne, G.L. (1995) Green fluorescent protein as a vital marker and reporter of gene expression in Drosophila. Proc. Natl. Acad. Sci. USA 92, 7036- 7040.
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Tau Phosphorylation Sites Work in Concert to Promote Neurotoxicity In Vivo
Steinhilb, M. L., Dias-Santagata, D., Fulga, T. A., Felch, D. L., & Feany, M. B. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-04-0327 · Cited by 187 · see citing works
Ando, K., Maruko-Otake, A., Ohtake, Y., Hayashishita, M., Sekiya, M., & Iijima, K. M. (2016) · PLOS Genetics · doi:10.1371/journal.pgen.1005917 · Cited by 105 · see citing works
- Authors
- Grammenoudi, S., Kosmidis, S., & Skoulakis, E. M. C.
- Affiliations
- Alexander Fleming Biomedical Sciences Research Center (GR)
- Corresponding author
- Skoulakis, Efthimios M.C.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2006-07-21
- Volume
- 580
- Issue
- 19
- Pages
- 4602-4606
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2159224793
- Cited by
- 29
- References
- 1
- Citations by year
- 2025: 1 · 2020: 2 · 2019: 2 · 2018: 3 · 2017: 3 · 2016: 2 · 2014: 1 · 2013: 1 · 2012: 2
- FWCI
- 1.05
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Commission
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neurobiology and Insect Physiology Research
- Keywords
- tau protein, tau phosphorylation, tauopathy, cell type-specific gene expression, Drosophila, neuronal cell types, protein stability, neurodegeneration
- MeSH terms
- Animals, Brain, Drosophila, Eye, Humans, Protein Processing, Post-Translational, Recombinant Proteins, tau Proteins, Animals, Genetically Modified
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