Pin1 affects Tau phosphorylation in response to Abeta oligomers.

@article{Bulbarelli2009Pin1AT,
  title={Pin1 affects Tau phosphorylation in response to Abeta oligomers.},
  author={Alessandra Bulbarelli and Elena Lonati and Emanuela Cazzaniga and Maria Gregori and Massimo Masserini},
  journal={Molecular and cellular neurosciences},
  year={2009},
  volume={42 1},
  pages={75-80}
}
We show that in hippocampal cultured neurons, dephosphorylation of peptidyl-prolyl cis-trans isomerase Pin1 on Ser16 is occurring during the early stages of exposure to Abeta (1-42) oligomers. This occurrence, resulting in Pin1 activation, is paralleled by Tau(Thr231) dephosphorylation, probably due to Pin1-mediated Tau isomerisation. Indeed, in the presence of the specific Pin1 inhibitor juglone, Abeta-induced Tau(Thr231)dephosphorylation is prevented. The involvement of protein phosphatase 2A… CONTINUE READING
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