Complementation of the mitotic activator, p80cdc25, by a human protein-tyrosine phosphatase
1990
Gould, K.L. | Moreno, S. | Tonks, N.K. | Nurse, P.
The onset of M phase requires the activation of the pp34 protein kinase in all eukaryotes thus far examined. In Schizosaccharomyces pombe, pp34 is phosphorylated on Tyr(15), and dephosphorylation of this residue regulates the initiation of mitosis. In this study, it is shown that dephosphorylation of Tyr(15) triggered activation of the pp34-cyclin complex from fission yeast, that a human protein-tyrosine phosphatase can catalyze this event both in vitro and in vivo, and that activation of fission yeast pp34 does not require threonine dephosphorylation. The complementary DNA that encoded the tyrosine phosphatase replaced the mitotic activator p80(cdc25), closely associating the cdc25+-activating pathway with tyrosine dephosphorylation of pp34.
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