Interaction between tau and alpha-synuclein proteins is impaired in the presence of P301L tau mutation

Luisa Benussi, Roberta Ghidoni, Anna Paterlini, Francesca Nicosia, Antonella C. Alberici, Simona Signorini, Laura Barbiero, Giuliano Binetti

Research output: Contribution to journalArticlepeer-review

Abstract

Deposits of tau and alpha-synuclein are hallmarks of distinct neurodegenerative diseases: tauopathies and alpha-synucleinopathies. Affinity chromatography experiments demonstrated a direct binding of the two proteins, and alpha-synuclein was shown to induce fibrillization of tau. Here, we verify the presence of this physical interaction by using different cellular systems. This binding was abolished by the most common tau mutation (P301L) associated with frontotemporal dementia. We restored the impaired interaction by inducing heat shock proteins 70 and 90. In addition, we show that P301L tau mutation strongly affects tau and alpha-synuclein neuronal distribution.

Original languageEnglish
Pages (from-to)78-84
Number of pages7
JournalExperimental Cell Research
Volume308
Issue number1
DOIs
Publication statusPublished - Aug 1 2005

Keywords

  • Alpha-synuclein
  • Alpha-synucleinopathies
  • Confocal microscopy
  • Familial frontotemporal dementia
  • Heat shock protein
  • Parkinson disease
  • Protein-protein interaction
  • Tau
  • Tau mutation (P301L)
  • Tauopathies

ASJC Scopus subject areas

  • Cell Biology

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