Molecular Biology of the Cell track citations

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print January 31, 2007
Mol. Biol. Cell 10.1091/mbc.E06-06-0510

A more recent version of this article appeared on April 1, 2007
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E06-06-0510v1
18/4/1242    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hatzoglou, A.
Right arrow Articles by de Gunzburg, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hatzoglou, A.
Right arrow Articles by de Gunzburg, J.

Submitted on June 9, 2006
Revised on December 7, 2006
Accepted on January 18, 2007

Gem Associates with Ezrin and Acts via the Rho-GAP Protein Gmip to Down-regulate the Rho Pathway

Anastassia Hatzoglou,*{dagger}{ddagger} Isabelle Ader,*{dagger}{sect} Anne Splingard,*{dagger} James Flanders,*{dagger}|| Evelyne Saade,*{dagger} Ingrid Leroy,*{dagger} Sabine Traver,*{dagger} Sandra Aresta,*{dagger} and Jean de Gunzburg*{dagger}

*Institut Curie-Centre de Recherche and {dagger}Inserm U528, Paris F-75248, France

Monitoring Editor: J. Silvio Gutkind

Gem is a protein of the Ras superfamily that plays a role in regulating voltage-gated Ca2+ channels and cytoskeletal reorganization. We now report that GTP-bound Gem interacts with the membrane-cytoskeleton linker protein Ezrin in its active state, and that Gem binds to active Ezrin in cells. The coexpression of Gem and Ezrin induces cell elongation accompanied by the disappearance of actin stress fibers and collapse of most focal adhesions. The same morphological effect is elicited when cells expressing Gem alone are stimulated with serum, and requires the expression of ERM proteins. We show that endogenous Gem downregulates the level of active RhoA and actin stress fibers. The effects of Gem downstream of Rho, i.e., ERM phosphorylation as well as disappearance of actin stress fibers and most focal adhesions, require the Rho-GAP partner of Gem, Gmip. a protein that is enriched in membranes under conditions in which Gem induced cell elongation. Our results suggest that Gem binds active Ezrin at the plasma membrane-cytoskeleton interface, and acts via the Rho-GAP protein Gmip to down-regulate processes dependent on the Rho pathway.

Present addresses: {ddagger}LBCMCP, CNRS UMR5088, Université Paul Sabatier-Toulouse III, 118 Route de Narbonne, 31062 Toulouse Cedex 9, France; {sect}INSERM U563, Institut Claudius Regaud, 20-24 Rue du Pont St Pierre, 31052 Toulouse Cedex, France; ||Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853; Inserm UMR599, 27 Bd. Leï Roure, 13009 Marseille, France.

Address correspondence to: Anastassia Hatzoglou (hatzoglo{at}cict.fr) or Jean de Gunzburg (gunzburg{at}curie.fr)






Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2007 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.