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J Biol Chem, Vol. 273, Issue 27, 16782-16786, July 3, 1998
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From the The Rac and Cdc42 GTPases regulate diverse
cellular behaviors involving the actin cytoskeleton, gene
transcription, and the activity of multiple protein and lipid kinases.
All of these pathways can potentially become activated when GTP-Rac or
GTP-Cdc42 is formed in response to external cell signals, yet it is
evident that each activity must also be able to be controlled
individually. The mechanisms by which such specificity of GTPase
signaling in response to upstream stimuli is achieved remains unclear.
We investigated the action of several well characterized guanine
nucleotide exchange factors (GEFRho) to activate Rac-
and/or Cdc42-dependent kinase pathways. Coexpression studies in COS-7 cells revealed that the ability of individual guanine
nucleotide exchange factors (GEFs) to activate the p21-activated kinase
PAK1 could be dissociated from activation of c-Jun amino-terminal kinase, even though activation of both pathways requires the action of
the GEFs on Rac and/or Cdc42. In contrast, expression of constitutively active forms of Rac or Cdc42 effectively stimulated both downstream kinases. We conclude that GEFs can be important determinants of downstream signaling specificity for members of the Rho GTPase family.
Departments of Immunology and Cell Biology,
The Scripps Research Institute, La Jolla, California 92037, the
¶ Department of Pediatrics, University of Michigan, Ann Arbor,
Michigan 48109, and ** Cell Biology, The Netherlands Cancer Institute,
121 Plesmaniaan, Amsterdam, The Netherlands 1066CS
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