PubMed: 22926167

Tau pathology modulates Pin1 post-translational modifications and may be relevant as biomarker.
Neurobiology of aging
Landrieu I | Lippens G | Buée L | Ando K | Galas MC | Bégard S | Sergeant N | Blum D | Bretteville A | Bélarbi K | Caillet-Boudin ML | Demey-Thomas E | Dourlen P | Drobecq H | Eddarkaoui S | Ghestem A | Hamdane M | Maurage CA | Melnyk P | Sambo AV | Smet C | Verdier Y | Vingtdeux V | Vinh J

Evidence 40cff85b57

Because Pin1 has at least 4 major isovariants in addition to the native polypeptide, this means that Pin1 has 4 (possibly more) posttranslational modifications including phosphorylation at 3 sites (Ser16 and Ser65/Ser71), N-acetylation (amino-terminus and Lys46) and oxidation (Met130 and 146). In all experimental conditions, including tau-overexpressing cells, tau transgenic mice and AD brains, global levels of Pin1 posttranslational modifications were decreased compared with control conditions.

Evidence 2f3abf11a9

Pin1 binds to phosphorylated Thr231 of tau and facilitates the dephosphorylation of phosphoThr231 through isomerization (Galas et al., 2006; Hamdane et al., 2006; Lu et al., 1999a). Phosphorylation at Thr231 on tau is associated with the early events of tau aggregation and NFT (Augustinack et al., 2002). Pin1 binds and isomerizes the proline imidic peptide bond following the phosphothreonine 231

Evidence 661e0a35c4

In fact, phosphorylation of Pin1 at Ser16 inhibits its nuclear localization possibly through inhibition of Pin1 substrate-binding property (Lu et al., 2002) while phosphorylation at Ser65 does not change activity of localization but stabilizes Pin1 by preventing its ubiquitination


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