J. Gautier, M.J. Solomon, R.N. Booher, J.F. Bazan, M.W. Kirschner, "cdc25 is a specific tyrosine phosphatase that directly activates p34 cdc2," Cell, 67:197-211, 1991.
Jean Gautier (Station Zoologique, Villefranche sur mer, France): "Cell cycle regulation at the onset of mitosis is controlled by the activation of MPF, a complex formed by the p34cdc2 protein kinase, plus a regulatory cyclin subunit. The final step of this activation process is the removal of at least one inhibitory phosphate group on the tyrosine 15 residue of the p34cdc2 molecule. Although previous genetic and biochemical data suggested that this final activation step was carried out by the cdc25 molecule, no convincing evidence that cdc25 directly dephosphoryl-ated p34cdc2 was available. Known protein tyrosine phosphatases (PTPs) shared significant structural homology, but cdc25 did not match most PTP characteristics based on sequence analysis.
"In our paper, we demonstrated that the cdc25 protein was able to directly dephosphorylate ...
