International Journal of Alzheimer s Disease · 2012 · 120 citations · 69 references
Life SciencesBiochemistryMolecular BiologyNeurodegenerationPost-translational ModificationProtein BiochemistryProtein AggregationProtein Aggregation DisordersProtein PhosphorylationProtein TurnoverTau PathologyAmino AcidsSerine PhosphorylationTau HyperphosphorylationTau Post-translational ModificationsTau Protein AggregationTau ToxicityTau-associated NeurotoxicityThreonine Phosphorylation
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.
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A protein factor essential for microtubule assembly.
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