PubMed:7644510 JSONTXT

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":31,"end":36},"obj":"protein"},{"id":"T2","span":{"begin":55,"end":60},"obj":"protein"},{"id":"T3","span":{"begin":741,"end":746},"obj":"protein"},{"id":"T4","span":{"begin":891,"end":896},"obj":"protein"},{"id":"T5","span":{"begin":980,"end":986},"obj":"protein"},{"id":"T6","span":{"begin":1076,"end":1082},"obj":"protein"},{"id":"T7","span":{"begin":1102,"end":1107},"obj":"protein"},{"id":"T8","span":{"begin":1159,"end":1164},"obj":"protein"},{"id":"T9","span":{"begin":1170,"end":1175},"obj":"protein"}],"text":"14-3-3 proteins associate with cdc25 phosphatases.\nThe cdc25 phosphatases play key roles in cell cycle progression by activating cyclin-dependent kinases. Two members of the 14-3-3 protein family have been isolated in a yeast two-hybrid screen designed to identify proteins that interact with the human cdc25A and cdc25B phosphatases. Genes encoding the human homolog of the 14-3-3 epsilon protein and the previously described 14-3-3 beta protein have been isolated in this screening. 14-3-3 proteins constitute a family of well-conserved eukaryotic proteins that were originally isolated in mammalian brain preparations and that possess diverse biochemical activities related to signal transduction. We present evidence that indicates that cdc25 and 14-3-3 proteins physically interact both in vitro and in vivo. 14-3-3 protein does not, however, affect the phosphatase activity of cdc25A. Raf-1, which is known to bind 14-3-3 proteins, has recently been shown to associate with cdc25A and to stimulate its phosphatase activity. 14-3-3 protein, however, has no effect on the cdc25A-kinase activity of Raf-1. Instead, 14-3-3 may facilitate the association of cdc25 with Raf-1 in vivo, participating in the linkage between mitogenic signaling and the cell cycle machinery."}