Raf1 interaction with Cdc25 phosphatase ties mitogenic signal transduction to cell cycle activation.
The Ras and Raf1 proto-oncogenes transduce extracellular signals that promote cell growth. Cdc25 phosphatases activate the cell division cycle by dephosphorylation of critical threonine and tyrosine residues within the cyclin-dependent kinases. We show here that Cdc25 phosphatase associates with raf1 in somatic mammalian cells and in meiotic frog oocytes. Furthermore, ... Cdc25 phosphatase can be activated in vitro in a Raf1-dependent manner. We suggest that activation of the cell cycle by the Ras/Raf1 pathways might be mediated in part by Cdc25.
Mesh Terms:
Amino Acid Sequence, Animals, Cell Cycle, Cell Cycle Proteins, Cell Extracts, Cell Line, Cell Membrane, Fibroblasts, Hela Cells, Humans, Meiosis, Molecular Sequence Data, Oocytes, Phosphoprotein Phosphatases, Phosphorylation, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-raf, Recombinant Fusion Proteins, Signal Transduction, Spodoptera, Xenopus, cdc25 Phosphatases
Amino Acid Sequence, Animals, Cell Cycle, Cell Cycle Proteins, Cell Extracts, Cell Line, Cell Membrane, Fibroblasts, Hela Cells, Humans, Meiosis, Molecular Sequence Data, Oocytes, Phosphoprotein Phosphatases, Phosphorylation, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-raf, Recombinant Fusion Proteins, Signal Transduction, Spodoptera, Xenopus, cdc25 Phosphatases
Genes Dev.
Date: May. 01, 1995
PubMed ID: 7744247
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