Background |
Phosphoinositide-dependent protein kinase 1 (PDK1) plays a central role in many signal transduction pathways including the activation of Akt and the PKC isoenzymes p70 S6 kinase and RSK. Through its effects on these kinases, PDK1 is involved in the regulation of a wide variety of processes, including cell proliferation, differentiation and apoptosis.Several serine sites (Ser25, Ser241, Ser393/396 and Ser410) are phosphorylated on PDK1 in unstimulated human embryo kidney 293 cells, as well as IGF-1 stimulated cells. Phosphorylation on the activation loop Ser241 by autophosphorylation is necessary for PDK1 activity.
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