JCB logo
amgmicro.com
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article
Right arrow Full Text
Right arrow Full Text (PDF, 547K)
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 Tuxworth, R. I.
Right arrow Articles by Insall, R. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tuxworth, R. I.
Right arrow Articles by Insall, R. H.
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, 0021-9525/1997//605 $5.00
The Journal of Cell Biology, Volume 138, Number 3, , 1997 605-614


Article

Dictyostelium RasG Is Required for Normal Motility and Cytokinesis, But Not Growth



Richard I. Tuxworth*,{ddagger}, Janet L. Cheetham*,{ddagger}, Laura M. Machesky*,§, George B. Spiegelmann||, Gerald Weeks||, and Robert H. Insall*,{ddagger}

* Medical Research Council Laboratory for Molecular Cell Biology, {ddagger} Department of Physiology, and § Department of Molecular Medicine, University College London, London WC1E 6BT, United Kingdom; and || Department of Microbiology and Immunology and Department of Medical Genetics, University of British Columbia, Vancouver V6T 1Z3, Canada

RasG is the most abundant Ras protein in growing Dictyostelium cells and the closest relative of mammalian Ras proteins. We have generated null mutants in which expression of RasG is completely abolished. Unexpectedly, RasG cells are able to grow at nearly wild-type rates. However, they exhibit defective cell movement and a wide range of defects in the control of the actin cytoskeleton, including a loss of cell polarity, absence of normal lamellipodia, formation of unusual small, punctate polymerized actin structures, and a large number of abnormally long filopodia. Despite their lack of polarity and abnormal cytoskeleton, mutant cells perform normal chemotaxis. However, rasG cells are unable to perform normal cytokinesis, becoming multinucleate when grown in suspension culture. Taken together, these data suggest a principal role for RasG in coordination of cell movement and control of the cytoskeleton.


1. Abbreviations used in this paper: GAP, GTPase-activating protein; GEF, guanine nucleotide exchange factors.

The work described in this paper was supported by a Wellcome Trust Career Development Fellowship 043754 to R.H. Insall, by a Medical Research Council Career Development Fellowship to L.M. Machesky, and by a grant from the Medical Research Council of Canada to G. Weeks. R.I. Tuxworth is supported by the Medical Research Council graduate program from the Institute of Molecular Cell Biology, University College London.

Please address all correspondence to Robert Insall, MRC Laboratory for Molecular Cell Biology, University College London, Gower Street, London WC1E 6BT, UK. Tel.: (44) 171 380 7270; Fax: (44) 171 380 7805; E-mail: dmcbrob{at}ucl.ac.uk



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