Learn More
Cdc25B is a phosphatase that catalyzes the dephosphorylation and activation of the cyclin-dependent kinases, thus driving cell cycle progression. We have identified two residues, R488 and Y497, located >20 A from the active site, that mediate protein substrate recognition without affecting activity toward small-molecule substrates. Injection of Cdc25B(More)
The Cdc25 phosphatases function as key regulators of the cell cycle during normal eukaryotic cell division and as mediators of the checkpoint response in cells with DNA damage. The role of Cdc25s in cancer has become increasingly evident in recent years. More than 20 studies of patient samples from diverse cancers show significant overexpression of Cdc25(More)
Cdc25 phosphatases are key activators of the eukaryotic cell cycle and compelling anticancer targets because their overexpression has been associated with numerous cancers. However, drug discovery targeting these phosphatases has been hampered by the lack of structural information about how Cdc25s interact with their native protein substrates, the(More)
Myt1 is a dual-specificity kinase that contributes to the regulation of the cell cycle by adding inhibitory phosphates to the cyclin-dependent kinases (Cdk/cyclins). Myt1 is found to be phosphorylated and less active in M-phase compared to interphase. Although Myt1 can be phosphorylated by several different kinases in vitro, it is not well understood how(More)
Protein phosphorylation is the mediator of many important cellular processes of signal transduction and cell regulation. Phosphorylation often occurs on multiple sites within a single protein, whereby the results of individual phosphorylations are not well defined. This is partially due to the lack of tools for analyzing specific phosphorylation states in a(More)
  • 1