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

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Isoform specific phosphorylation of protein phosphatase 2C expressed in COS7 cells.

Of the six distinct isoforms of mouse protein phosphatase 2C (PP2C) (alpha, beta-1, beta-2, beta-3, beta-4 and beta-5), PP2C alpha was specifically phosphorylated on the serine residue(s) when expressed in COS7 cells. Analysis of phosphorylation sites using site-directed mutagenesis demonstrated that Ser-375 and/or Ser-377 were phosphorylated in vivo. These serine residues were the sites of phosphorylation by casein kinase II in vitro. Phosphorylation of PP2C alpha was enhanced two-fold by the addition of okadaic acid to the culture medium, but addition of cyclosporin A had no such effect. These results suggest that the expressed PP2C alpha is phosphorylated by a casein kinase II-like protein kinase and dephosphorylated by PP1 and/or PP2A in COS7 cells.[1]

References

  1. Isoform specific phosphorylation of protein phosphatase 2C expressed in COS7 cells. Kobayashi, T., Kusuda, K., Ohnishi, M., Wang, H., Ikeda, S., Hanada, M., Yanagawa, Y., Tamura, S. FEBS Lett. (1998) [Pubmed]
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