Journal
DEVELOPMENTAL CELL
Volume 13, Issue 5, Pages 646-662Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2007.08.011
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Funding
- NIGMS NIH HHS [GM39434, R01 GM071868, R01 GM044428, GM67230, U54 GM64346, GM44428, R01 GM039434-20, U54 GM064346, U01 GM067230, R01 GM039434, R01 GM044428-17, R01 GM067230, R01 GM071868-02] Funding Source: Medline
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Protrusion of the leading edge of migrating epithelial cells requires precise regulation of two actin filament (F-actin) networks, the lamellipodium and the lamella. Cofilin is a downstream target of Rho GTPase signaling that promotes F-actin cycling through its F-actin-nucleating, -severing, and -depolymerizing activity. However, its function in modulating lamellipodium and lamella dynamics, and the implications of these dynamics for protrusion efficiency, has been unclear. Using quantitative fluorescent speckle microscopy, immunofluorescence, and electron microscopy, we establish that the Rac1/Pak1/LIMK1 signaling pathway controls cofilin activity within the lamellipodium. Enhancement of cofilin activity accelerates F-actin turnover and retrograde flow, resulting in widening of the lamellipodium. This is accompanied by increased spatial overlap of the lamellipodium and lamella networks and reduced cell-edge protrusion efficiency. We propose that cofilin functions as a regulator of cell protrusion by modulating the spatial interaction of the lamellipodium and lamella. in response to upstream signals.
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