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Vol. 9, Issue 6, 1379-1394, June 1998
and
IGMM, CNRS-UMR5535, Route de Mende, 34293 Montpellier Cedex 05 France
RhoG is a member of the Rho family of GTPases that shares 72% and
62% sequence identity with Rac1 and Cdc42Hs, respectively. We have
expressed mutant RhoG proteins fused to the green fluorescent protein
and analyzed subsequent changes in cell surface morphology and
modifications of cytoskeletal structures. In rat and mouse fibroblasts,
green fluorescent protein chimera and endogenous RhoG proteins
colocalize according to a tubular cytoplasmic pattern, with perinuclear
accumulation and local concentration at the plasma membrane.
Constitutively active RhoG proteins produce morphological and
cytoskeletal changes similar to those elicited by a simultaneous activation of Rac1 and Cdc42Hs, i.e., the formation of ruffles, lamellipodia, filopodia, and partial loss of stress fibers. In addition, RhoG and Cdc42Hs promote the formation of microvilli at the
cell apical membrane. RhoG-dependent events are not mediated through a
direct interaction with Rac1 and Cdc42Hs targets such as PAK-1, POR1,
or WASP proteins but require endogenous Rac1 and Cdc42Hs activities:
coexpression of a dominant negative Rac1 impairs membrane ruffling and
lamellipodia but not filopodia or microvilli formation. Conversely,
coexpression of a dominant negative Cdc42Hs only blocks microvilli and
filopodia, but not membrane ruffling and lamellipodia. Microtubule
depolymerization upon nocodazole treatment leads to a loss of RhoG
protein from the cell periphery associated with a reversal of the RhoG
phenotype, whereas PDGF or bradykinin stimulation of nocodazole-treated
cells could still promote Rac1- and Cdc42Hs-dependent cytoskeletal
reorganization. Therefore, our data demonstrate that RhoG controls a
pathway that requires the microtubule network and activates Rac1 and
Cdc42Hs independently of their growth factor signaling pathways.
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