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Vol. 18, Issue 10, 3723-3732, October 2007
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*Laboratory of Cell Biophysics, Ecole Polytechnique Fédérale de Lausanne, 1015 Lausanne, Switzerland;
Unité Mixte de Recherche 144, Institut Curie, 75248 Paris, France; and
Physopathologie et Thérapeutique Respiratoires, Institut National de la Santé et de la Recherche Médicale Unité Mixte de Recherche 492, 94010 Créteil, France
Submitted September 25, 2006;
Revised June 18, 2007;
Accepted July 9, 2007
Monitoring Editor: Ted Salmon
To understand the mechanism of cell migration, one needs to know how the parts of the motile machinery of the cell are assembled and how they move with respect to each other. Actin and myosin II are thought to be the major structural and force-generating components of this machinery (Mitchison and Cramer, 1996; Parent, 2004). The movement of myosin II along actin filaments is thought to generate contractile force contributing to cell translocation, but the relative motion of the two proteins has not been investigated. We use fluorescence speckle and conventional fluorescence microscopy, image analysis, and computer tracking techniques to generate comparative velocity and assembly maps of actin and myosin II over the entire cell in a simple model system of persistently migrating fish epidermal keratocytes. The results demonstrate contrasting polarized assembly patterns of the two components, indicate force generation at the lamellipodium–cell body transition zone, and suggest a mechanism of anisotropic network contraction via sliding of myosin II assemblies along divergent actin filaments.
The online version of this article contains supplemental material MBC Online (http://www.molbiolcell.org).
These authors contributed equally to this work.
Address correspondence to: Alexander B. Verkhovsky (alexander.verkhovsky{at}epfl.ch)
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