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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Phosphorylation and activation of p40 tyrosine kinase by casein kinase-1.

Because examination of regulatory trans-phosphorylations can help elucidate the cellular functions of tyrosyl protein kinases, we have investigated the effects of phosphorylation by casein kinase-1 on the activity of the p40 tyrosyl protein kinase. We find that casein kinase-1 can phosphorylate the p40 tyrosyl kinase on serine and threonine residues, in part on a unique tryptic peptide. The phosphorylation induces a substantial increase in the tyrosyl protein kinase activity of p40, in contrast to most instances in which serine/threonine phosphorylation inhibits activity of tyrosyl protein kinases. These findings raise the possibility that p40 might be part of a protein phosphorylation network in which casein kinase-1 participates.[1]

References

  1. Phosphorylation and activation of p40 tyrosine kinase by casein kinase-1. Vila, J., Payne, D.M., Zioncheck, T.F., Harrison, M.L., Itarte, E., Weber, M.J. FEBS Lett. (1990) [Pubmed]
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