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International Journal of Alzheimer’s Disease
Volume 2012, Article ID 578373, 7 pages
Review Article

Tau Phosphorylation by GSK3 in Different Conditions

1Centro de Biologia Molecular “Severo Ochoa” (CSIC-UAM), Nicolás Cabrera 1, Campus Cantoblanco UAM, 28049 Madrid, Spain
2Centro de Investigación Biomédica en Red de Enfermedades neurodegenerativas (CIBERNED), 28031 Madrid, Spain
3Instituto Cajal, Consejo Superior de Investigaciones Científicas, I28002 Madrid, Spain
4Laboratorio Cajal de Circuitos Corticales, Centro de Tecnología Biomédica, Universidad Politécnica de Madrid, 28223 Madrid, Spain

Received 17 January 2012; Accepted 15 March 2012

Academic Editor: Hanna Rosenmann

Copyright © 2012 Jesús Avila et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.