JCB logo
Accuri Cytometers
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 14 February 2005. doi:10.1083/jcb.200406063
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 4, 619-631
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 6188K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
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 Gupton, S. L.
Right arrow Articles by Waterman-Storer, C. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gupton, S. L.
Right arrow Articles by Waterman-Storer, C. M.
Right arrowPubmed/NCBI databases
*Substance via MeSH
Related Collections
Right arrowRelated Article
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?

Article

Cell migration without a lamellipodium

: translation of actin dynamics into cell movement mediated by tropomyosin



Stephanie L. Gupton1, Karen L. Anderson2, Thomas P. Kole3, Robert S. Fischer1, Aaron Ponti1, Sarah E. Hitchcock-DeGregori4, Gaudenz Danuser1, Velia M. Fowler1, Denis Wirtz3, Dorit Hanein2, and Clare M. Waterman-Storer1

1 Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037
2 Program on Cell Adhesion, The Burnham Institute, La Jolla, CA 92037
3 Department of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD 21218
4 Department of Neuroscience and Cell Biology, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, NJ 08854

Correspondence to Clare Waterman-Storer: waterman{at}scripps.edu

The actin cytoskeleton is locally regulated for functional specializations for cell motility. Using quantitative fluorescent speckle microscopy (qFSM) of migrating epithelial cells, we previously defined two distinct F-actin networks based on their F-actin–binding proteins and distinct patterns of F-actin turnover and movement. The lamellipodium consists of a treadmilling F-actin array with rapid polymerization-dependent retrograde flow and contains high concentrations of Arp2/3 and ADF/cofilin, whereas the lamella exhibits spatially random punctae of F-actin assembly and disassembly with slow myosin-mediated retrograde flow and contains myosin II and tropomyosin (TM). In this paper, we microinjected skeletal muscle {alpha}TM into epithelial cells, and using qFSM, electron microscopy, and immunolocalization show that this inhibits functional lamellipodium formation. Cells with inhibited lamellipodia exhibit persistent leading edge protrusion and rapid cell migration. Inhibition of endogenous long TM isoforms alters protrusion persistence. Thus, cells can migrate with inhibited lamellipodia, and we suggest that TM is a major regulator of F-actin functional specialization in migrating cells.

Abbreviations used in this paper: FSM, fluorescent speckle microscopy; qFSM, quantitative FSM; skTM; skeletal muscle {alpha}TM; TM, tropomyosin.


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?

Related Article

Lamellae lead the way
Rabiya S. Tuma
J. Cell Biol. 2005 168: 520. [Full Text] [PDF]



This article has been cited by other articles:



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