JCB logo
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 732K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nobes, C. D.
Right arrow Articles by Chardin, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nobes, C. D.
Right arrow Articles by Chardin, P.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© The Rockefeller University Press, 0021-9525/1998//187 $5.00
The Journal of Cell Biology, Volume 141, Number 1, , 1998 187-197

Regular Articles

A New Member of the Rho Family, Rnd1, Promotes Disassembly of Actin Filament Structures and Loss of Cell Adhesion



Catherine D. Nobes§, Inger Lauritzen*, Marie-Geneviève Mattei{ddagger}, Sonia Paris*, Alan Hall§, and Pierre Chardin*

* Institut de Pharmacologie, Centre National de la Recherche Scientifique UPR 411, 06560 Valbonne, France; {ddagger} Institut National de la Sante et de la Recherche Medicale U.406, Faculté de Médecine de la Timone, 13385 Marseille Cedex, France; and § Medical Research Council Laboratory for Molecular Cell Biology, Cancer Research Campaign Oncogene and Signal Transduction Group and Department of Biochemistry, University College London, London WC1E 7BT, United Kingdom

Members of the Rho GTPase family regulate the organization of the actin cytoskeleton in response to extracellular growth factors. We have identified three proteins that form a distinct branch of the Rho family: Rnd1, expressed mostly in brain and liver; Rnd2, highly expressed in testis; and Rnd3/RhoE, showing a ubiquitous low expression. At the subcellular level, Rnd1 is concentrated at adherens junctions both in confluent fibroblasts and in epithelial cells. Rnd1 has a low affinity for GDP and spontaneously exchanges nucleotide rapidly in a physiological buffer. Furthermore, Rnd1 lacks intrinsic GTPase activity suggesting that in vivo, it might be constitutively in a GTP-bound form. Expression of Rnd1 or Rnd3/RhoE in fibroblasts inhibits the formation of actin stress fibers, membrane ruffles, and integrin-based focal adhesions and induces loss of cell–substrate adhesion leading to cell rounding (hence Rnd for "round"). We suggest that these proteins control rearrangements of the actin cytoskeleton and changes in cell adhesion.

Abbreviations used in this paper: GEF, guanine nucleotide exchange factors; GAP, GTPase-activating proteins; LPA, lysophosphatidic acid; REF, rat embryo fibroblast.

C.D. Nobes and A. Hall were supported by the Cancer Research Campaign (UK). P. Chardin's work in A. Hall's laboratory was supported by a short term European Molecular Biological Organisation fellowship.

Address all correspondence to Pierre Chardin's present address, Cancer Center, University of California, 2340 Sutter Street, San Francisco, CA 94115. Fax: (415) 502-3179. E-mail: chardin{at}cc.ucsf.edu


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents