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

doi:10.1016/j.yexcr.2005.04.021

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

Centro San Giovanni di Dio - Fatebenefratelli

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	78-84
Number of pages	7
Journal	Experimental Cell Research
Volume	308
Issue number	1
DOIs	https://doi.org/10.1016/j.yexcr.2005.04.021
Publication status	Published - 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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10.1016/j.yexcr.2005.04.021

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Interaction between tau and alpha-synuclein proteins is impaired in the presence of P301L tau mutation. / Benussi, Luisa ; Ghidoni, Roberta; Paterlini, Anna; Nicosia, Francesca; Alberici, Antonella C.; Signorini, Simona; Barbiero, Laura; Binetti, Giuliano.

In: Experimental Cell Research, Vol. 308, No. 1, 01.08.2005, p. 78-84.

Research output: Contribution to journal › Article › peer-review

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

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.",

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AU - Benussi, Luisa

AU - Ghidoni, Roberta

AU - Paterlini, Anna

AU - Nicosia, Francesca

AU - Alberici, Antonella C.

AU - Signorini, Simona

AU - Barbiero, Laura

AU - Binetti, Giuliano

PY - 2005/8/1

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N2 - 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.

AB - 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.

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KW - Familial frontotemporal dementia

KW - Heat shock protein

KW - Parkinson disease

KW - Protein-protein interaction

KW - Tau

KW - Tau mutation (P301L)

KW - Tauopathies

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

Abstract

Keywords

ASJC Scopus subject areas

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