Cell type-specific processing of human Tau proteins in Drosophila.
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.
Grammenoudi
Sofia
S
Institute of Molecular Biology and Genetics, Biomedical Sciences Research Centre "Alexander Fleming", 34 Fleming Street, Vari 16672, Greece.
Kosmidis
Stylianos
S
Skoulakis
Efthimios M C
EM
D000818:Animals; D030801:Animals, Genetically Modified; D001921:Brain / Q000378:metabolism; D004330:Drosophila / Q000235:genetics*; D005123:Eye / Q000378:metabolism; D006801:Humans; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D016875:tau Proteins / Q000235:genetics* / Q000378:metabolism
D011994:Recombinant Proteins; D016875:tau Proteins