Article
Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation.
Molecular and cellular biology - 1 Mar 2005
Scheid Michael P, Parsons Michael, Woodgett James R
Abstract excerpt
3-phosphoinositide-dependent kinase 1 (PDK1) phosphorylates the activation loop of a number of protein serine/threonine kinases of the AGC kinase superfamily, including protein kinase B (PKB; also called Akt), serum and glucocorticoid-induced kinase, protein kinase C isoforms, and the p70 ribosomal S6 kinase. PDK1 contains a carboxyl-terminal pleckstrin homology domain, which targets phosphoinositide lipids at...
Topics
- 3-Phosphoinositide-Dependent Protein Kinases
- Active Transport, Cell Nucleus
- Amino Acid Motifs
- Amino Acid Sequence
- Animals
- Cell Line
- Cell Membrane
- Cell Nucleus
- DNA-Binding Proteins
- Down-Regulation
- Fatty Acids, Unsaturated
- Forkhead Box Protein O1
- Forkhead Transcription Factors