help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Originally published as Biophys J. BioFAST on September 3, 2004.
doi:10.1529/biophysj.104.047589
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow supplemental file
Right arrow All Versions of this Article:
biophysj.104.047589v1
87/5/3493    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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gerisch, G.
Right arrow Articles by Anderson, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gerisch, G.
Right arrow Articles by Anderson, K.
Biophysical Journal 87:3493-3503 (2004)
© 2004 The Biophysical Society

Mobile Actin Clusters and Traveling Waves in Cells Recovering from Actin Depolymerization

Günther Gerisch *, Till Bretschneider *, Annette Müller-Taubenberger *, Evelyn Simmeth *, Mary Ecke *, Stefan Diez {dagger} and Kurt Anderson {dagger}

* Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany; and {dagger} Max-Planck-Institut für molekulare Zellbiologie und Genetik, D-01307 Dresden, Germany

Correspondence: Address reprint requests to Günther Gerisch, Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany. Tel.: 49-89-8578-2326; Fax: 49-89-8578-3885; E-mail: gerisch{at}biochem.mpg.de.

At the leading edge of a motile cell, actin polymerizes in close apposition to the plasma membrane. Here we ask how the machinery for force generation at a leading edge is established de novo after the global depolymerization of actin. The depolymerization is accomplished by latrunculin A, and the reorganization of actin upon removal of the drug is visualized in Dictyostelium cells by total internal reflection fluorescence microscopy. The actin filament system is reorganized in three steps. First, F-actin assembles into globular complexes that move along the bottom surface of the cells at velocities up to 10 µm/min. These clusters are transient structures that eventually disassemble, fuse, or divide. In a second step, clusters merge into a contiguous zone at the cell border that spreads and gives rise to actin waves traveling on a planar membrane. Finally, normal cell shape and motility are resumed. These data show that the initiation of actin polymerization is separated in Dictyostelium from front protrusion, and that the coupling of polymerization to protrusion is a later step in the reconstitution of a leading edge.




This article has been cited by other articles:


Home page
 J. Cell Sci.Home page
K. Murthy and P. Wadsworth
Dual role for microtubules in regulating cortical contractility during cytokinesis
J. Cell Sci., July 15, 2008; 121(14): 2350 - 2359.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
H. Patel, I. Konig, M. Tsujioka, M. C. Frame, K. I. Anderson, and V. G. Brunton
The multi-FERM-domain-containing protein FrmA is required for turnover of paxillin-adhesion sites during cell migration of Dictyostelium
J. Cell Sci., April 15, 2008; 121(8): 1159 - 1164.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
N. S. Gov and A. Gopinathan
Dynamics of Membranes Driven by Actin Polymerization
Biophys. J., January 15, 2006; 90(2): 454 - 469.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2004 by the Biophysical Society.