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PubMed: 22926167

Title
Tau pathology modulates Pin1 post-translational modifications and may be relevant as biomarker.
Journal
Neurobiology of aging
Volume
34
Issue
None
Pages
757-69
Date
2013-03-01
Authors
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
JSON

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.

p(HGNC:MAPT) negativeCorrelation p(HGNC:PIN1, pmod(Ph, Ser, 71)) View Subject | View Object

Appears in Networks:

p(HGNC:MAPT) negativeCorrelation p(HGNC:PIN1, pmod(Ph, Ser, 16)) View Subject | View Object

Appears in Networks:

p(HGNC:MAPT) negativeCorrelation p(HGNC:PIN1, pmod(Ph, Ser, 65)) View Subject | View Object

Appears in Networks:

p(HGNC:MAPT) negativeCorrelation p(HGNC:PIN1, pmod(Ac, Lys, 46)) View Subject | View Object

Appears in Networks:

p(HGNC:PIN1, pmod(Ac, Lys, 46)) negativeCorrelation p(HGNC:MAPT) View Subject | View Object

Appears in Networks:

p(HGNC:PIN1, pmod(Ph, Ser, 16)) negativeCorrelation p(HGNC:MAPT) View Subject | View Object

Appears in Networks:

p(HGNC:PIN1, pmod(Ph, Ser, 65)) negativeCorrelation p(HGNC:MAPT) View Subject | View Object

Appears in Networks:

p(HGNC:PIN1, pmod(Ph, Ser, 71)) negativeCorrelation p(HGNC:MAPT) View Subject | View Object

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Evidence 2f3abf11a9
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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

p(HGNC:MAPT, pmod(Ph, Thr, 231)) increases a(HBP:"Tau aggregates") View Subject | View Object

Appears in Networks:

act(p(HGNC:PIN1)) directlyDecreases p(HGNC:MAPT, pmod(Ph, Thr, 231)) View Subject | View Object

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Evidence 661e0a35c4
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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

p(HGNC:PIN1, pmod(Ph, Ser, 16)) decreases act(p(HGNC:PIN1)) View Subject | View Object

Appears in Networks:

p(HGNC:PIN1, pmod(Ph, Ser, 65)) increases act(p(HGNC:PIN1)) View Subject | View Object

Appears in Networks:

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.