Association of p-S216-CDC25C with 14-3-3 proteins

Stable Identifier
Reaction [binding]
Homo sapiens
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CDC25C is phosphorylated by CHK1 at ser-216 (Blasina et al.,1999 ) resulting in both inhibition of the CDC25 phosphatase activity and creation of a 14-3-3 docking site (Peng et al., 1997). Association of 14-3-3 proteins with phosphorylated CDC25C (p-S216-CDC25C) is thought to result in retention of this complex within the cytoplasm (Dalal et al., 1999; Graves et al, 2001).

Literature References
PubMed ID Title Journal Year
10330186 Cytoplasmic localization of human cdc25C during interphase requires an intact 14-3-3 binding site.

DeCaprio, JA, Schweitzer, CM, Gan, J, Dalal, SN

Mol Cell Biol 1999
11313932 Localization of human Cdc25C is regulated both by nuclear export and 14-3-3 protein binding.

Piwnica-Worms, H, Lovly, CM, Uy, GL, Graves, PR

Oncogene 2001
9278512 Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216.

Piwnica-Worms, H, Shaw, AS, Thoma, RS, Peng, CY, Wu, Z, Graves, PR

Science 1997
9889122 A human homologue of the checkpoint kinase Cds1 directly inhibits Cdc25 phosphatase

McGowan, CH, Luyten, WH, Parker, AE, Blasina, A, de Weyer, IV, Laus, MC

Curr Biol 1999
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