Interaction of the protein kinase Raf-1 with 14-3-3 proteins.
Members of a family of highly conserved proteins, termed 14-3-3 proteins, were found by several experimental approaches to associate with Raf-1, a central component of a key signal transduction pathway. Optimal complex formation required the amino-terminal regulatory domain of Raf-1. The association of 14-3-3 proteins and Raf-1 was not substantially affected by the activation state of Raf.
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Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.
Xia
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Pallas
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Cui
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Conroy
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Narsimhan
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Mamon
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Collier
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Roberts
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D048948:14-3-3 Proteins; D016475:3T3 Cells; D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D004789:Enzyme Activation; D006801:Humans; D051379:Mice; D009419:Nerve Tissue Proteins / Q000378:metabolism; D010766:Phosphorylation; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D011518:Proto-Oncogene Proteins / Q000378:metabolism*; D019908:Proto-Oncogene Proteins c-raf; D015398:Signal Transduction; D018411:Spodoptera; D014446:Tyrosine 3-Monooxygenase; D016335:Zinc Fingers
D048948:14-3-3 Proteins; D009419:Nerve Tissue Proteins; D011506:Proteins; D011518:Proto-Oncogene Proteins; D014446:Tyrosine 3-Monooxygenase; D011065:Poly(ADP-ribose) Polymerases; D017346:Protein Serine-Threonine Kinases; D019908:Proto-Oncogene Proteins c-raf