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The lamellipodium is the actin-rich foremost region of the leading edge of a migrating cell. This highly dynamic structure promotes cell migration through protrusion formation driven by actin polymerisation at the plasma membrane.
Actin polymerization in lamellipodia of cells is regulated by the Arp2/3 complex and FMNL family formins. Here the authors show that both FMNL2 and FMNL3 contribute to lamellipodium protrusion and structure, and abolishing FMNL2/3 reduces protrusion force generation and migration, without affecting Arp2/3 incorporation.
In animal cells, actin is dynamically distributed between multiple coexisting arrays. Carlier and Shekhar propose that a global treadmilling process — whereby the various actin networks grow and shrink depending on the local activity of actin regulators — establishes a steady-state concentration of actin monomers that supports this homeostatic actin turnover.