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Vol. 13, Issue 3, 902-914, March 2002
-induced Mobilization of Actin
Cytoskeleton Requires Signaling by Small GTPases Cdc42 and RhoA
Ludwig Institute for Cancer Research, Biomedical Center, S-751 24 Uppsala, Sweden
Transforming growth factor-
(TGF-) is a potent regulator of
cell growth and differentiation in many cell types. The Smad signaling
pathway constitutes a main signal transduction route downstream of
TGF- receptors. We studied TGF--induced rearrangements of the
actin filament system and found that TGF-1 treatment of PC-3U human
prostate carcinoma cells resulted in a rapid formation of lamellipodia.
Interestingly, this response was shown to be independent of the Smad
signaling pathway; instead, it required the activity of the Rho GTPases
Cdc42 and RhoA, because ectopic expression of dominant negative mutant
Cdc42 and RhoA abrogated the response. Long-term stimulation with
TGF-1 resulted in an assembly of stress fibers; this response
required both signaling via Cdc42 and RhoA, and Smad proteins. A known
downstream effector of Cdc42 is p38MAPK; treatment of the
cells with the p38MAPK inhibitor
4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(pyridyl)1H-imidazole (SB203580), as well as ectopic expression of a kinase-inactive p38MAPK, abrogated the TGF--induced actin
reorganization. Moreover, treatment of cells with the inhibitors of the
RhoA target-protein Rho-associated coiled-coil kinase
(+)-R-trans-4-(aminoethyl)-N-(4-pyridyl) cyclohexanecarboxamide (Y-27632) and
1-5(-isoquinolinesulfonyl)homopiperazine (HA-1077), as well as ectopic
expression of kinase-inactive Rho coiled-coil kinase-1,
abrogated the TGF-1-induced formation of stress fibers.
Collectively, these data indicate that TGF--induced membrane
ruffles occur via Rho GTPase-dependent pathways, whereas long-term
effects require cooperation between Smad and Rho GTPase signaling pathways.
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