Abstract
Epidermal growth factor (EGF), insulin-like growth factor 1 (IGF1) and phorbol myristate acetate (PMA) induce the inhibition of glycogen synthase kinase 3 (GSK3) by stimulating the phosphorylation of an N-terminal serine. Here, we show that protein kinase B (PKB) plays a key role in mediating EGF- induced inhibition of GSK3α and that the classical MAP kinase (MAPK) cascade has two functions in this process. Firstly, it makes a transient contribution to EGF-induced inhibition of GSK3α. Secondly, it shortens the duration of PKB activation and GSK3α inhibition. In contrast, PKB alone mediates the IGF1-induced inhibition of GSK3α, while the MAPK cascade mediates the inhibition of GSK3α by PMA.
Original language | English |
---|---|
Pages (from-to) | 120-124 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 461 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 12 Nov 1999 |
Keywords
- Epidermal growth factor
- Glycogen synthase kinase 3
- Insulin
- MAP kinase
- Protein kinase B
ASJC Scopus subject areas
- Structural Biology
- Biophysics
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology