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Volume 271, Number 28, Issue of July 12, 1996 pp. 16674-16677
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Role of the Raf/Mitogen-activated Protein Kinase Pathway in p21ras Desensitization

(Received for publication, January 31, 1996, and in revised form, April 24, 1996)

Jes K. Klarlund , Andrew D. Cherniack , Martin McMahon Dagger and Michael P. Czech

From the Program in Molecular Medicine and Department of Biochemistry and Molecular Biology, University of Massachusetts Medical Center, Worcester, Massachusetts 01605 and the Dagger  DNAX Research Institute of Molecular and Cellular Biology, Inc., Palo Alto, California 94304-1104

Desensitization of p21ras after stimulation of cells by growth factors and phorbol 12-myristate 13-acetate (PMA) correlates with hyperphosphorylation of the guanine nucleotide exchange factor Son-of-sevenless (Sos) and its dissociation from the adaptor protein Grb2 (Cherniack, A., Klarlund, J. K., Conway, B. R., and Czech, M. P. (1995) J. Biol. Chem. 270, 1485-1488). To test the role of the Raf/mitogen-activated protein (MAP) kinase pathway, we utilized cells expressing a chimera composed of the catalytic domain of p74Raf-1 and the hormone binding domain of the estradiol receptor (Delta Raf-1:ER). Estradiol markedly stimulated Delta Raf-1:ER and the downstream MEK and MAP kinases in these cells as well as Sos phosphorylation. However, the dissociation of Grb2 from Sos observed in response to PMA was not apparent upon Delta Raf-1:ER activation. Furthermore, stimulation of Delta Raf-1:ER did not impair GTP loading of p21ras in response to platelet-derived growth factor or epidermal growth factor. We conclude that activation of the Raf/MAP kinase pathway alone in these cells is insufficient to cause disassembly of Sos from Grb2 or to interrupt the ability of Sos to catalyze activation of p21ras.


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