p(HGNC:PIN1, frag("5_39")) association p(HGNC:MAPT, pmod(Ph, Thr, 231))

View Subject View Object

PubMed:10391244

In contrast, no binding was observed between Pin1 and the nonphosphorylated tau (Fig. 4a), demonstrating that T231 phosphorylation is required for Pin1 binding of tau. To determine whether the WW domain of Pin1 is responsible for binding, the mutant Pin1Y23A was used, which contains a single alanine substitution at the critical Tyr 23 in theWWdomain, resulting in a loss of the phosphoserine-binding activity13. Pin1Y23A showed much less binding to pT231 peptide (Table 1). The residual binding might be due to binding of the pT231 peptide to the much lower affinity isomerase domain of Pin113. These results indicate that the WW domain mediates Pin1 binding to the pT231 sequence of tau.

Related Edges 4

• complex(p(HGNC:MAPT, pmod(Ph, Thr, 231)), p(HGNC:PIN1, frag("5_39"))) positiveCorrelation act(p(HGNC:PIN1, frag("5_39")))
• p(HGNC:MAPT, pmod(Ph, Thr, 231)) association p(HGNC:PIN1, frag("5_39"))
• act(p(HGNC:PIN1, frag("5_39"))) positiveCorrelation complex(p(HGNC:MAPT, pmod(Ph, Thr, 231)), p(HGNC:PIN1, frag("5_39")))
• p(HGNC:PIN1, var("p.Tyr23Ala")) decreases act(p(HGNC:PIN1, frag("5_39")))

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

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.

---