CK2 phosphorylation of Pdx-1 regulates its transcription factor activity
✍ Scribed by Rui Meng; Faizeh Al-Quobaili; Isabelle Müller; Claudia Götz; Gerald Thiel; Mathias Montenarh
- Publisher
- Springer
- Year
- 2010
- Tongue
- English
- Weight
- 517 KB
- Volume
- 67
- Category
- Article
- ISSN
- 1420-682X
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## Abstract Phosphorylation of phospholipase C‐δ~1~ (PLC‐δ~1~) in vitro and in vivo was investigated. Of the serine/threonine kinases tested, protein kinase C (PKC) phosphorylated the serine residue(s) of bacterially expressed PLC‐δ~1~ most potently. It was also demonstrated that PLC‐δ~1~ directly
β-Catenin is a key protein in the canonical Wnt signaling pathway and in many cancers alterations in transcriptional activity of its components are observed. This pathway is up-regulated by the protein kinase CK2, but the underlying mechanism of this change is unknown. It has been demonstrated that