Zeta 14-3-3 protein favours the formation of human tau fibrillar polymers

被引：59

作者：

Hernández, F ^{[1
]}

Cuadros, R ^{[1
]}

Avila, J ^{[1
]}

机构：

[1] Univ Autonoma Madrid, Fac Ciencias, Ctr Biol Mol Severo Ochoa, CSIC, E-28049 Madrid, Spain

来源：

NEUROSCIENCE LETTERS | 2004年 / 357卷 / 02期

关键词：

Alzheimer's disease; paired helical filaments; Tau; phosphorylation; 14-3-3;

D O I：

10.1016/j.neulet.2003.12.049

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

Tau protein can aggregate, in an aberrant way, in Alzheimer's disease and other tauopathies. The formation of those aggregates could take place in vitro by the addition of different compounds like polyanions or fatty acids and their derivates. Now, we found that a protein, zeta 14-3-3, facilitates the assembly of tau as well as a tau peptide containing the self-assembly region of tau molecule and a site for PKA phosphorylation. Also, we have found that tau and tau peptide polymerization are reduced, but not abolished upon PKA phosphorylation. The involvement of a scaffolding protein like 14-3-3 in the generation of tau filaments in tauopathies, like AD, is suggested. (C) 2004 Elsevier Ireland Ltd. All rights reserved.

引用

页码：143 / 146

页数：4

共 27 条

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