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

Stable Identifier
R-HSA-75016
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

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

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

Oncogene 2001
10330186 Cytoplasmic localization of human cdc25C during interphase requires an intact 14-3-3 binding site.

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

Mol Cell Biol 1999
9278512 Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216.

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

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

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

Curr Biol 1999
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