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J. Biol. Chem., Vol. 275, Issue 42, 33046-33052, October 20, 2000
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From the Centre de Recherche de Biochimie Macromoléculaire,
CNRS, UPR 1086, 1919 Route de Mende, Montpellier 34293, Cedex,
France
In this study we show that expression of active
Cdc42Hs and Rac1 GTPases, two Rho family members, leads to the
reorganization of the vimentin intermediate filament (IF) network,
showing a perinuclear collapse. Cdc42Hs displays a stronger effect than Rac1 as 90% versus 75% of GTPase-expressing cells show
vimentin collapse. Similar vimentin IF modifications were observed when endogenous Cdc42Hs was activated by bradykinin treatment, endogenous Rac1 by platelet-derived growth factor/epidermal growth factor, or both
endogenous proteins upon expression of active RhoG. This reorganization
of the vimentin IF network is not associated with any significant
increase in soluble vimentin. Using effector loop mutants of Cdc42Hs
and Rac1, we show that the vimentin collapse is mostly independent of
CRIB (Cdc42Hs or Rac-interacting binding)-mediated pathways such as JNK
or PAK activation but is associated with actin reorganization. This
does not result from F-actin depolymerization, because cytochalasin D
treatment or Scar-WA expression have merely no effect on
vimentin organization. Finally, we show that genistein treatment of
Cdc42 and Rac1-expressing cells strongly reduces vimentin collapse,
whereas staurosporin, wortmannin, LY-294002, Rp-cAMP, or RII, the regulatory subunit
of protein kinase A, remain ineffective. Moreover, we detected an
increase in cellular tyrosine phosphorylation content after Cdc42Hs and
Rac1 expression without modification of the vimentin phosphorylation
status. These data indicate that Cdc42Hs and Rac1 GTPases control
vimentin IF organization involving tyrosine phosphorylation events.
Cdc42Hs and Rac1 GTPases Induce the Collapse of the Vimentin
Intermediate Filament Network*
,,
*
This work was supported by the Association
Française contre les Myopathies, the Association pour la
Recherche contre le Cancer (Contract 9759), the Ligue Nationale contre
le Cancer, and the Fondation pour la Recherche Médicale.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Both authors contributed equally to this work.
§
To whom correspondence should be addressed. Tel.: 33-4-67-61-33-55;
Fax: 33-4-67-52-15-59; E-mail: gauthier@crbm.cnrs-mop.fr.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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