Tau Phosphorylation by GSK3 in Different Conditions-Reference-Cited by-同舟云学术

Tau Phosphorylation by GSK3 in Different Conditions

Published:2012 Issue: Volume:2012 Page:1-7
ISSN:2090-8024
Container-title:International Journal of Alzheimer's Disease
language:en
Short-container-title:International Journal of Alzheimer's Disease

Author:

Avila Jesús¹²,León-Espinosa Gonzalo²³⁴,García Esther¹²,García-Escudero Vega¹²,Hernández Félix¹²,DeFelipe Javier²³⁴

Affiliation:

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

2. Centro de Investigación Biomédica en Red de Enfermedades neurodegenerativas (CIBERNED), 28031 Madrid, Spain

3. Instituto Cajal, Consejo Superior de Investigaciones Científicas, I28002 Madrid, Spain

4. Laboratorio Cajal de Circuitos Corticales, Centro de Tecnología Biomédica, Universidad Politécnica de Madrid, 28223 Madrid, Spain

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.

Publisher

Hindawi Limited

Subject

Behavioral Neuroscience,Cellular and Molecular Neuroscience,Cognitive Neuroscience,Neurology (clinical),Neurology,Aging,General Medicine

Link

http://downloads.hindawi.com/journals/ijad/2012/578373.pdf

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