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J Biol Chem, Vol. 274, Issue 7, 4430-4439, February 12, 1999

Characterization of Raf-1 Activation in Mitosis

A. Douglas LairdDagger , Deborah K. Morrison§, and David ShallowayDagger

From the Dagger  Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853 and the § Molecular Basis of Carcinogenesis Laboratory, Advanced Biosciences Laboratories, Basic Research Program, NCI-Frederick Cancer Research and Development Center, Frederick, Maryland 21702

We have used site-directed mutagenesis to explore the mechanisms underlying Raf-1 activation in mitosis, and we have excluded most previously characterized activating interactions. Our results indicate that the primary locus of activation lies in the carboxyl-half of the molecule, although the extent of activation can be influenced by the amino-proximal region, particularly by the Raf-1 zinc finger. We also found that Raf-1 is hyperphosphorylated in mitosis at multiple sites within residues 283-302 and that these hyperphosphorylations are not required for activation. In addition, neither Mek1 nor Mek2 are stably activated in coordination with Raf-1 in nocodazole-arrested cells. Overall, the data suggest that the mechanism(s) responsible for activating Raf-1 during mitosis, and the subsequent downstream effects, are distinct from those involved in growth factor stimulation.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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