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不同条件下糖原合酶激酶3介导的tau蛋白磷酸化

Tau Phosphorylation by GSK3 in Different Conditions.

作者信息

Avila Jesús, León-Espinosa Gonzalo, García Esther, García-Escudero Vega, Hernández Félix, Defelipe Javier

机构信息

Centro de Biologia Molecular "Severo Ochoa" (CSIC-UAM), Nicolás Cabrera 1, Campus Cantoblanco UAM, 28049 Madrid, Spain.

出版信息

Int J Alzheimers Dis. 2012;2012:578373. doi: 10.1155/2012/578373. Epub 2012 May 17.

Abstract

Almost a 20% of the residues of tau protein are phosphorylatable amino acids: serine, threonine, and tyrosine. In this paper we comment on the consequences for tau of being a phosphoprotein. We will focus on serine/threonine phosphorylation. It will be discussed that, depending on the modified residue in tau molecule, phosphorylation could be protective, in processes like hibernation, or toxic like in development of those diseases known as tauopathies, which are characterized by an hyperphosphorylation and aggregation of tau.

摘要

tau蛋白近20%的残基是可磷酸化的氨基酸:丝氨酸、苏氨酸和酪氨酸。在本文中,我们阐述了tau作为一种磷蛋白所产生的影响。我们将聚焦于丝氨酸/苏氨酸磷酸化。将讨论的是,根据tau分子中被修饰的残基不同,磷酸化在诸如冬眠等过程中可能具有保护作用,而在那些被称为tau蛋白病的疾病发展过程中则可能具有毒性,tau蛋白病的特征是tau蛋白的过度磷酸化和聚集。

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