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

被引：30

作者：

Benussi, L ^{[1
]}

Ghidoni, R ^{[1
]}

Paterlini, A ^{[1
]}

Nicosia, F ^{[1
]}

Alberici, AC ^{[1
]}

Signorini, S ^{[1
]}

Barbiero, L ^{[1
]}

Binetti, G ^{[1
]}

机构：

[1] IRCCS, Ctr S Giovanni Dio FBF, NeuroBioGen Lab Memory Clin, I-25123 Brescia, Italy

来源：

EXPERIMENTAL CELL RESEARCH | 2005年 / 308卷 / 01期

关键词：

familial frontotemporal dementia; Parkinson disease; tauopathies; alpha-synucleinopathies; tau; alpha-synuclein; tau mutation (P301L); protein-protein interaction; heat shock protein; confocal microscopy;

D O I：

10.1016/j.yexcr.2005.04.021

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

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. (c) 2005 Elsevier Inc. All rights reserved.

引用

页码：78 / 84

页数：7

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