A common denominator linking glycogen metabolism, nuclear oncogenes and development.
A ubiquitous protein-serine kinase, initially implicated in glycogen regulation, has surfaced unexpectedly in the fields of nuclear oncogenes and fruitfly development. This unusual linkage may reflect the role of this kinase in phosphorylating proteins normally activated by dephosphorylation, thus providing a priming function. Loss of such a primer would result in constitutive activation of substrates, a scenario concordant with the dramatic and pleiotropic phenotype observed in Drosophila null mutants.
Woodgett
J R
JR
Ludwig Institute for Cancer Research, London, UK.
D000595:Amino Acid Sequence; D000818:Animals; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D004330:Drosophila / Q000235:genetics; D006003:Glycogen / Q000378:metabolism*; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011494:Protein Kinases / Q000235:genetics / Q000378:metabolism; D011518:Proto-Oncogene Proteins / Q000235:genetics / Q000378:metabolism*; D016755:Proto-Oncogene Proteins c-jun; D020598:Proto-Oncogene Proteins c-myb; D012689:Sequence Homology, Nucleic Acid; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*
D004268:DNA-Binding Proteins; D011518:Proto-Oncogene Proteins; D016755:Proto-Oncogene Proteins c-jun; D020598:Proto-Oncogene Proteins c-myb; D014157:Transcription Factors; D006003:Glycogen; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases