Title

Pin1 promotes degradation of Smad proteins and their interaction with phosphorylated tau in Alzheimer's disease.

Journal

Neuropathology and applied neurobiology

Volume

40

Issue

None

Pages

815-32

Date

2014-12-01

Authors

Arendt T | Brückner MK | Gruschka H | Hilbrich I | Holzer M | Rohn S | Ueberham E | Ueberham U | Wodischeck S

Alltogether, this provides evidence for a negative feed-back regulation of Pin1 by Smad. A similar mechanism might be instrumental in AD, where nuclear Smad concentrations are significantly reduced , which potentially contributes to increased levels of Pin1 [16]

The high degree of colocalization between pSmad2/3 and ubiquitin (Figure 7) provides additional evidence for a forced degradation of Smad2 via the proteasome pathway in AD which is controlled through binding of Pin1

The results demonstrate a direct interaction of Smad2 with phospho-tau (Figure 8B) which is clearly enhanced in the presence of Pin1.

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.