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Phosphorylated, but not native, tau protein assembles following reaction with the lipid peroxidation product,
M Pérez1, R Cuadros, M A Smith
1Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid, Spain.
FEBS Letters
|December 20, 2000
Abstract:
A correlation between hyperphosphorylation of tau protein and its aberrant assembly into paired helical filaments has lead to suggestions that phosphorylation controls assembly, but lacked a mechanistic basic. In this work, we have found that phosphorylated, but not native, tau protein is able to form polymers after the reaction with 4-hydroxy-2-nonenal, a highly toxic product of lipid peroxidation. Phosphorylation of tau by both proline or non-proline directed kinases, was able to assemble it into polymers.