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Published 14 February 2005. doi:10.1083/jcb.200406063
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 4, 619-631
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 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.


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