Deletion of endogenous Tau proteins is not detrimental in Drosophila

Sylvie Burnouf, Sebastian Grönke, Hrvoje Augustin, Jacqueline Dols, Marianna Karina Gorsky, Jennifer Werner, Fiona Kerr, Nazif Alic, Pedro Martinez, Linda Partridge

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)
12 Downloads (Pure)


Human Tau (hTau) is a highly soluble and natively unfolded protein that binds to microtubules within neurons. Its dysfunction and aggregation into insoluble paired helical filaments is involved in the pathogenesis of Alzheimer’s disease (AD), constituting, together with accumulated ß-amyloid (Aß) peptides, a hallmark of the disease. Deciphering both the loss-of-function and toxic gain-of-function of hTau proteins is crucial to further understand the mechanisms leading to neurodegeneration in AD. As the fruit fly Drosophila melanogaster expresses Tau proteins (dTau) that are homologous to hTau, we aimed to better comprehend dTau functions by generating a specific tau knock-out (KO) fly line using homologous recombination. We observed that the specific removal of endogenous dTau proteins did not lead to overt, macroscopic phenotypes in flies. Indeed, survival, climbing ability and neuronal function were unchanged in tau KO flies. In addition, we did not find any overt positive or negative effect of dTau removal on human Aß-induced toxicity. Altogether, our results indicate that the absence of dTau proteins has no major functional impact on flies, and suggests that our tau KO strain is a relevant model to further investigate the role of dTau proteins in vivo, thereby giving additional insights into hTau functions.
Original languageEnglish
JournalScientific Reports
Publication statusPublished - 15 Mar 2016


  • hTau
  • Alzheimer's disease
  • Tau proteins
  • Drosophila
  • neurodegenerative diseases


Dive into the research topics of 'Deletion of endogenous Tau proteins is not detrimental in Drosophila'. Together they form a unique fingerprint.

Cite this