Binding of 14-3-3 Proteins to the Protein Kinase Raf and Effects on Its Activation
Autor: | Frank McCormick, Marc Symons, S. G. Macdonald, Ellen Freed, Rosamaria Ruggieri |
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Rok vydání: | 1994 |
Předmět: |
MAPK/ERK pathway
Tyrosine 3-Monooxygenase Molecular Sequence Data MAP Kinase Kinase 1 Nerve Tissue Proteins Saccharomyces cerevisiae Protein Serine-Threonine Kinases Mitogen-activated protein kinase kinase Biology Cell Line Cytosol GTP-Binding Proteins Proto-Oncogene Proteins Animals Humans Amino Acid Sequence c-Raf Protein kinase A Mitogen-Activated Protein Kinase Kinases Multidisciplinary Cell Membrane Zinc Fingers Protein phosphatase 2 Protein-Tyrosine Kinases Recombinant Proteins Enzyme Activation Proto-Oncogene Proteins c-raf 14-3-3 Proteins Protein kinase domain Biochemistry Signal transduction HeLa Cells Signal Transduction |
Zdroj: | Science. 265:1713-1716 |
ISSN: | 1095-9203 0036-8075 |
DOI: | 10.1126/science.8085158 |
Popis: | To identify proteins that may participate in the activation of the protein kinase Raf, proteins that interact with Raf were selected in a two-hybrid screen. Two members of the 14-3-3 protein family were isolated that interacted with both the amino terminal regulatory regions of Raf and the kinase domain of Raf, but did not compete with the guanine nucleotide-binding protein Ras for binding to Raf. 14-3-3 proteins associated with Raf in mammalian cells and accompanied Raf to the membrane in the presence of activated Ras. In yeast cells expressing Raf and MEK, mammalian 14-3-3 beta or 14-3-3 zeta activated Raf to a similar extent as did expression of Ras. Therefore, 14-3-3 proteins may participate in or be required for the regulation of Raf function. These findings suggest a role for 14-3-3 proteins in Raf-mediated signal transduction. |
Databáze: | OpenAIRE |
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