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• W297874522 abstract "Research Article15 February 1995free access Regulation of Raf-1 kinase activity by the 14-3-3 family of proteins. S. Li S. Li Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author P. Janosch P. Janosch Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author M. Tanji M. Tanji Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author G.C. Rosenfeld G.C. Rosenfeld Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author J.C. Waymire J.C. Waymire Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author H. Mischak H. Mischak Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author W. Kolch W. Kolch Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author J.M. Sedivy J.M. Sedivy Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author S. Li S. Li Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author P. Janosch P. Janosch Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author M. Tanji M. Tanji Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author G.C. Rosenfeld G.C. Rosenfeld Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author J.C. Waymire J.C. Waymire Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author H. Mischak H. Mischak Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author W. Kolch W. Kolch Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author J.M. Sedivy J.M. Sedivy Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. Search for more papers by this author Author Information S. Li1, P. Janosch1, M. Tanji1, G.C. Rosenfeld1, J.C. Waymire1, H. Mischak1, W. Kolch1 and J.M. Sedivy1 1Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520. The EMBO Journal (1995)14:685-696https://doi.org/10.1002/j.1460-2075.1995.tb07047.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info We have identified the beta (beta) isoform of the 14-3-3 family of proteins as an activator of the Raf-1 protein kinase. 14-3-3 was isolated in a yeast two-hybrid screen for Raf-1 kinase domain binding proteins. Purified bovine brain 14-3-3 interacted specifically with both c-Raf-1 and the isolated Raf-1 kinase domain. Association was sensitive to the activation status of Raf-1; 14-3-3 bound to unactivated Raf-1, but not Raf-1 activated by protein kinase C alpha or Ras and Lck. The significance of these interactions under physiological conditions was demonstrated by co-immunoprecipitation of Raf-1 and 14-3-3 from extracts of quiescent, but not mitogen-stimulated, NIH 3T3 cells. 14-3-3 was not a preferred Raf-1 substrate in vitro and did not significantly affect Raf-1 kinase activity in a purified system. However, in cell-free extracts 14-3-3 acted as a Ras-independent activator of both c-Raf-1 and the Raf-1 kinase domain. The same results were obtained in vivo using transfection assays; 14-3-3 enhanced both c-Raf-1- and Raf-1 kinase domain-stimulated expression of AP-1- and NF-kappa B-dependent reporter genes and accelerated Raf-1 kinase domain-triggered differentiation of PC12 cells. We conclude that 14-3-3 is a latent co-activator bound to unactivated Raf-1 in quiescent cells and mediates mitogen-triggered but Ras-independent regulatory effects aimed directly at the kinase domain. Previous ArticleNext Article Volume 14Issue 41 February 1995In this issue RelatedDetailsLoading ..." @default.
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• W297874522 date "1995-02-01" @default.
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• W297874522 title "Regulation of Raf-1 kinase activity by the 14-3-3 family of proteins." @default.
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• W297874522 doi "https://doi.org/10.1002/j.1460-2075.1995.tb07047.x" @default.
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