Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization.
The Raf-1 serine/threonine kinase is a key component of the MAP kinase cascade, regulating both proliferation and commitment to cell fate. Raf activation is stimulated following its translocation to the plasma membrane, a process that ordinarily requires interaction with the membrane-localized GTPase, Ras-GTP. To investigate the mechanisms underlying Raf activation, we have developed a coumermycin-induced chemical dimerization method. We find that dimerization is by itself sufficient, in the absence of any membrane components, both to activate a modified Raf protein and to stimulate the MAP kinase cascade appropriately. As Ras-GTP-induced membrane localization increases the effective intracellular Raf concentration, our results indicate that homotypic oligomerization may ordinarily act to promote Raf activation in vivo.[1]References
- Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization. Farrar, M.A., Alberol-Ila, n.u.l.l., Perlmutter, R.M. Nature (1996) [Pubmed]
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