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• W2024981492 startingPage "7892" @default.
• W2024981492 abstract "The 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." @default.
• W2024981492 created "2016-06-24" @default.
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• W2024981492 date "1995-08-15" @default.
• W2024981492 modified "2023-10-17" @default.
• W2024981492 title "14-3-3 proteins associate with cdc25 phosphatases." @default.
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• W2024981492 doi "https://doi.org/10.1073/pnas.92.17.7892" @default.
• W2024981492 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/41252" @default.
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