PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2

Background: Protein kinase B (PKB) is activated by phosphorylation of Thr308 and of Ser473. Thr308 is phosphorylated by the 3-phosphoinositide-dependent protein kinase-1 (PDK1) but the identity of the kinase that phosphorylates Ser473 (provisionally termed PDK2) is unknown. Results: The kinase domai...

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Veröffentlicht in:	Current biology 1999-04, Vol.9 (8), p.393-404
Hauptverfasser:	Balendran, Anudharan, Casamayor, Antonio, Deak, Maria, Paterson, Andrew, Gaffney, Piers, Currie, Richard, Downes, C.Peter, Alessi, Dario R.
Format:	Artikel
Sprache:	eng
Schlagworte:	3-Phosphoinositide-Dependent Protein Kinases Amino Acid Sequence Animals Binding Sites Cell Line Enzyme Activation Glutathione Transferase - genetics Humans Isoenzymes - metabolism Lipids - physiology Molecular Sequence Data Peptides - chemical synthesis Peptides - genetics Peptides - metabolism Phosphatidylinositol Phosphates - physiology Phosphorylation Phosphoserine - metabolism Phosphothreonine - metabolism Protein Binding Protein Kinase C - chemistry Protein Kinase C - genetics Protein Kinase C - metabolism Protein-Serine-Threonine Kinases - metabolism Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-akt Rats Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Saccharomyces cerevisiae - genetics Sensitivity and Specificity Sequence Homology, Amino Acid Substrate Specificity
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