Activation of mouse 3-phosphoinositide-dependent protein kinase-1 (mPDK1) requires phosphorylation at a conserved serine residue, Ser 244 , in the activation loop. However, the mechanism by which mPDK1 is phosphorylated at this site remains unclear. We have found that kinase-defective mPDK1 (mPDK1 KD ), but not a kinasedefective mPDK1 in which Ser 244 was replaced with alanine (mPDK1 KD/S244A ), is significantly phosphorylated in intact cells and is a direct substrate of wild-type mPDK1 fused to the yellow fl…
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