Activation of Cdc25C

Stable Identifier
Homo sapiens
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PLK1 phosphorylates CDC25C on serine residue S198. In addition to catalytically activating CDC25C, PLK1-mediated phosphorylation also results in the nuclear accumulation of CDC25C (Toyoshima-Morimoto et al. 2002). It has been shown that Xenopus polo homolog, Plx1, directly phosphorylates and activates Cdc25C, which in turn dephosphorylates and activates Cdc2. This step is critical for the onset of mitosis. Since Plx1-dependent Cdc25C phosphorylation occurs in the absence of Cdc2 activity, it is likely that Plx1 is a triggering kinase, which leads to the activation of Cdc2 and therefore the normal onset of mitosis (Kumagai and Dunphy 1996).

Literature References
PubMed ID Title Journal Year
8703070 Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts

Kumagai, A

Science 1996
11897663 Plk1 promotes nuclear translocation of human Cdc25C during prophase

Toyoshima-Morimoto, F, Nishida, E, Taniguchi, E

EMBO Rep 2002
Event Information
Go Biological Process
Catalyst Activity

protein serine/threonine kinase activity of p-T210-PLK1 [cytosol]

Orthologous Events
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