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J Biol Chem, Vol. 274, Issue 4, 2279-2285, January 22, 1999
From the The possibility that the Dbl family member Lfc
can activate Rac1 in cells is investigated in this study. Previously,
we demonstrated that both Lfc and Lsc, like their closest relative Lbc,
can act catalytically in stimulating the guanine nucleotide exchange
activity of RhoA in vitro. Neither Lfc nor Lsc stimulated
the in vitro exchange activity of Cdc42 or Rac1; however,
Lfc was capable of forming a tight complex with Rac1 in
vitro. We show here that Lfc stimulates c-Jun kinase (JNK)
activity in COS-7 cells. This stimulation was blocked by a dominant
negative mutant of Rac1 and somewhat less effectively by dominant
negative RhoA, but not by dominant negative Cdc42. Overexpression of
Lfc in NIH 3T3 cells induced the formation of actin stress fibers and
membrane ruffles, consistent with the activation of both RhoA and Rac1
signaling pathways, whereas overexpression of Lsc led exclusively to
well developed stress fibers. Using a recently developed assay for measuring the cellular activation of Rac, we did not find that expression of Lfc increased the levels of GTP-bound Rac1. However, an
examination of the cellular localization of Lfc showed that it was
localized to microtubules, similar to what has been reported for
activated Rac1, the mixed lineage kinase (MLK) and JNK. Moreover, we
have found that the Pleckstrin homology (PH) domain of Lfc specifically
associates with tubulin. Taken together, these findings suggest a model
where the PH domain-mediated localization of Lfc to microtubules
enables the recruitment of Rac to a site proximal to its signaling
targets, resulting in JNK activation and actin cytoskeletal changes.
The Dbl-related Protein, Lfc, Localizes to Microtubules and
Mediates the Activation of Rac Signaling Pathways in Cells
,,
Department of Molecular Medicine, College of
Veterinary Medicine, Cornell University, Ithaca, New York 14853-6401, the § Department of Pharmacology and the Lineberger
Comprehensive Cancer Center, University of North Carolina, Chapel Hill,
North Carolina 27599, and the ¶ Terry Fox Laboratory, British
Columbia Cancer Agency, Vancouver,
British Columbia V5Z 4E6, Canada
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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