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Activation of Raf-1 by 14-3-3 proteins

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Abstract

THE protein Raf-1, a key mediator of mitogenesis and differentia-tion, associates with p21*"a5 (refs 1-3). However, the regulation of the serine/threonine kinase activity of Raf-1 is still not understood4 13. Using the yeast two-hybrid system8'14"16, we identi-fied two structurally related proteins that interact with the amino-terminal region of Raf-1. These proteins, 14-3-3 £ (PLA2) and 14-3-3 p (HS1), are members of the 14-3-3 family of proteins17'23. Expression of 14-3-3 proteins in Xenopm oocytes enhanced Raf-1 activity and promoted Raf-1-dependent oocyte maturation. A dominant negative mutant of Raf-1 blocked the effects of 14-3-3 protein.

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Author notes

  1. Anthony J. Muslin

    Present address: Cardiology Division, Department of Medicine, Jewish Hospital, Washington University Medical Center, St Louis, MO, 63110, USA

  2. Angus M. MacNicol

    Present address: University of Chicago, 5841 South Maryland Avenue, Chicago, IL, 60637, USA

  3. Wendy J. Fantl & Lewis T. Williams

    Present address: Chiron Corporation, Emeryville, CA, 94608, USA

  4. Richard W. Grosst: Division of Bioorganic Chemistry and Molecular Pharmacology, Washington University School of Medicine, St Louis, Missouri 63110, USA

Authors and Affiliations

  1. Daiichi Research Center, Cardiovascular Research Institute, Department of Medicine, University of California, San Francisco, California, 94143, USA

    Wendy J. Fantl, Anthony J. Muslin, Akira Kikuchi, Jay A. Martin, Angus M. MacNicol, Richard W. Grosst & Lewis T. Williams

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  1. Wendy J. Fantl
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  2. Anthony J. Muslin
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Fantl, W., Muslin, A., Kikuchi, A. et al. Activation of Raf-1 by 14-3-3 proteins. Nature 371, 612–614 (1994). https://doi.org/10.1038/371612a0

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