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Tau inhibits tubulin oligomerization induced by prion protein

Katarzyna M Osiecka1, Hanna Nieznanska, Krzysztof J Skowronek

  • 1Department of Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.

Biochimica Et Biophysica Acta
|July 19, 2011
PubMed

Insights

Microtubule-associated proteins (MAPs), like Tau, protect against prion protein (PrP)-induced tubulin damage. Tau phosphorylation impairs this protective effect, suggesting a link between transmissible spongiform encephalopathies and tauopathies.

Area of Science:

  • Neurobiology
  • Molecular Biology
  • Prion Disease Research

Background:

  • Prion protein (PrP) interacts with tubulin, disrupting the microtubular cytoskeleton via tubulin oligomerization.
  • This interaction may underlie the toxicity of cytoplasmic PrP in transmissible spongiform encephalopathies (TSEs).

Purpose of the Study:

  • To investigate the role of microtubule-associated proteins (MAPs) in modulating PrP-induced tubulin oligomerization.
  • To determine if Tau protein, a key MAP, influences PrP's effect on tubulin.

Main Methods:

  • Comparison of PrP-induced tubulin oligomerization in MAP-depleted versus MAP-containing tubulin preparations.
  • Assessment of Tau protein's effect on PrP-induced tubulin oligomerization.
  • Evaluation of the impact of Tau phosphorylation on its interaction with PrP and tubulin.

Main Results:

  • Tubulin preparations lacking MAPs were more susceptible to PrP-induced oligomerization.
  • Tau protein significantly reduced the oligomerization effect of PrP on tubulin.
  • Phosphorylation of Tau abolished its protective function against PrP-induced tubulin oligomerization.

Conclusions:

  • Tau protein binding stabilizes tubulin, making it less prone to PrP-induced oligomerization.
  • Altered Tau phosphorylation, common in Alzheimer disease and tauopathies, may compromise this protective mechanism.
  • Findings suggest a potential molecular link between TSEs and tauopathies, involving PrP and Tau interactions.

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