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Deregulation of PTEN/Akt signalling has been recently implicated in the pathogenesis of Alzheimer's disease (AD), but the effects on the molecular processes underlying AD pathology have not yet been fully described. Here we report that overexpression of PTEN reduces tau phosphorylation in CHO cells. This effect was abrogated by mutant PTEN constructs with either a catalytically inactive point mutation (C124S) or with only inactive lipid phosphatase activity (G129E), suggesting an indirect, lipid phosphatase-dependent process. The predominant effects of PTEN on tau appeared to be mediated by reducing ERK1/2 activity, but were independent of Akt, GSK-3, JNK and the tau phosphatases PP1 and PP2A. Our studies provide evidence for an effect of PTEN on the phosphorylation of tau in AD pathogenesis, and provide some insight into the mechanisms through which deregulation of PTEN may contribute towards the progression of tauopathy.

Original publication




Journal article



Publication Date





3121 - 3128


Alzheimer Disease, Animals, CHO Cells, Cerebral Cortex, Cricetinae, Cricetulus, Glycogen Synthase Kinase 3, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinase 3, Neurons, PTEN Phosphohydrolase, Phosphatidate Phosphatase, Phosphatidylinositol 3-Kinases, Phosphorylation, Point Mutation, Proto-Oncogene Proteins c-akt, tau Proteins