Kinase phosphorylation: Keeping it all in the family.
The identification of PDK1 as a kinase that phosphorylates the AGC family of kinases led to a hunt for 'PDK2', a hypothetical regulated kinase(s) that would be required for full activation of the AGC kinases. Recent findings suggest that the elusive PDK2 may actually be a familiar kinase with an atypical associate.
Howard Hughes Medical Institute, Departments of Chemistry and Chemical Biology and Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
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D064413:3-Phosphoinositide-Dependent Protein Kinases; D000595:Amino Acid Sequence; D017867:Cyclic Nucleotide-Regulated Protein Kinases / Q000378:metabolism* / Q000502:physiology*; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D008954:Models, Biological; D008969:Molecular Sequence Data; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000502:physiology; D011518:Proto-Oncogene Proteins / Q000737:chemistry / Q000378:metabolism; D051057:Proto-Oncogene Proteins c-akt; D017386:Sequence Homology, Amino Acid
D011518:Proto-Oncogene Proteins; D017867:Cyclic Nucleotide-Regulated Protein Kinases; D064413:3-Phosphoinositide-Dependent Protein Kinases; C578562:PDPK1 protein, human; D017346:Protein Serine-Threonine Kinases; D051057:Proto-Oncogene Proteins c-akt