Article
Regulation of phosphatidylinositol 3'-kinase by tyrosyl phosphoproteins. Full activation requires occupancy of both SH2 domains in the 85-kDa regulatory subunit.
The Journal of biological chemistry - 24 Feb 1995
Rordorf-Nikolic T, Van Horn D J, Chen D, White M F, Backer J M
Abstract excerpt
Phosphatidylinositol 3'-kinase (PI 3'-kinase) is activated in insulin-stimulated cells by the binding of the SH2 domains in its 85-kDa regulatory subunit to insulin receptor substrate-1 (IRS-1). We have previously shown that both tyrosyl-phosphorylated IRS-1 and mono-phosphopeptides containing a single YXXM motif activate PI 3'-kinase in vitro. However, activation by the monophosphopeptides was significantly less...
Topics
- Amino Acid Sequence
- Animals
- Cells, Cultured
- Cloning, Molecular
- Enzyme Activation
- Insulin Receptor Substrate Proteins
- Molecular Sequence Data
- Mutation
- Phosphatidylinositol 3-Kinases
- Phosphopeptides