p35/cdk5 binds and phosphorylates β-catenin and regulates β-catenin/presenilin-1 interaction
✍ Scribed by Sashi Kesavapany; Kwok-Fai Lau; Declan M. McLoughlin; Janet Brownlees; Steven Ackerley; P. Nigel Leigh; Christopher E. Shaw; Christopher C. J. Miller
- Book ID
- 109020310
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 187 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0953-816X
No coin nor oath required. For personal study only.
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## Abstract The cdk5/p35 complex has been implicated in a variety of functions related to brain development, including axonal outgrown and neuronal migration. In this study, by co‐immunoprecipitation and pull‐down experiments, we have shown that the cdk5/p35 complex associates with and phosphorylat
## Abstract CK2 is a regulatory kinase implicated in embryonic development and in cancer. Among the CK2 substrates is β‐catenin, a protein with dual function in Wnt signaling and cell adhesion. Previously, we reported that CK2 activity is required for β‐catenin stability and we identified threonine