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J Biol Chem, Vol. 273, Issue 52, 34954-34960, December 25, 1998
,
From the The Rho-related small GTPases are critical
elements involved in regulation of signal transduction cascades from
extracellular stimuli to cell nucleus and cytoskeleton. The Dbl-like
guanine nucleotide exchange factors (GEF) have been implicated in
direct activation of these GTPases. Here we have identified a new
member of the Dbl family, GEF-H1, by screening a human HeLa cell
cDNA library. GEF-H1 encodes a 100-kDa protein containing the
conserved structural array of a Dbl homology domain in tandem with a
pleckstrin homology domain and is most closely related to the
lfc oncogene, but additionally it contains a unique
coiled-coil domain at the carboxyl terminus. Biochemical analysis
reveals that GEF-H1 is capable of stimulating guanine nucleotide
exchange of Rac and Rho but is inactive toward Cdc42, TC10, or Ras.
Moreover, GEF-H1 binds to Rac and Rho proteins in both the GDP- and
guanosine 5'-3-O-(thio)triphosphate-bound states without
detectable affinity for Cdc42 or Ras. Immunofluorescence reveals that
GEF-H1 colocalizes with microtubules through the carboxyl-terminal
coiled-coil domain. Overexpression of GEF-H1 in COS-7 cells results in
induction of membrane ruffles. These results suggest that GEF-H1 may
have a direct role in activation of Rac and/or Rho and in bringing the
activated GTPase to specific target sites such as microtubules.
Department of Pharmacology, Baylor College
of Medicine, Houston, Texas 77030 and the ¶ Department of
Biochemistry, University of Tennessee, Memphis, Tennessee 38163
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