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Tau Phosphorylation

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Cytoskeleton of the Nervous System

Part of the book series: Advances in Neurobiology ((NEUROBIOL,volume 3))

Abstract

Tau protein is a brain microtubule–associated protein having 79 putative phosphorylatable sites that could be modified by serine/threonine protein kinases. This phosphorylation can be divided in two types, depending whether the modified residue is phosphorylated by proline-directed or by non-proline-directed protein kinases. In neurodegenerative processes (tauopathies), tau is mainly (but not only) modified by a proline-directed protein kinase, glycogen synthase kinase 3 (GSK3). In this chapter, we will review that phosphorylation at serine and threonine residues, the modification that can take place at tyrosine residues, and the dephosphorylation of the modified residues by tau phosphatases. In addition, we will comment on the toxicity of phosphotau in disorders such as Alzheimer’s disease and the development of possible therapies to prevent tau phosphorylation.

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  1. Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Universidad Autónoma de Madrid, 28049, Madrid, Spain

    Jesús Avila & Félix Hernández

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  1. Jesús Avila
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  2. Félix Hernández
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Correspondence to Jesús Avila .

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  1. Psychiatric Research, Nathan S. Kline Institute for, 140 Old Orangeburg Road, Orangeburg, 10962, New York, USA

    Ralph A. Nixon

  2. Psychiatric Research, Nathan S. Kline Institute for, 140 Old Orangeburg Road, Orangeburg, 10962, New York, USA

    Aidong Yuan

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Avila, J., Hernández, F. (2011). Tau Phosphorylation. In: Nixon, R., Yuan, A. (eds) Cytoskeleton of the Nervous System. Advances in Neurobiology, vol 3. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-6787-9_3

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