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Cellular motility driven by assembly and disassembly of actin filaments

Journal

CELL
Volume 112, Issue 4, Pages 453-465

Publisher

CELL PRESS
DOI: 10.1016/S0092-8674(03)00120-X

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Funding

  1. NIGMS NIH HHS [GM62431, GM26338] Funding Source: Medline

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Motile cells extend a leading edge by assembling a branched network of actin filaments that produces physical force, as the polymers grow beneath the plasma membrane. A core set of proteins including actin, Arp2/3 complex, profilin, capping protein, and ADF/cofilin can reconstitute the process in vitro, and mathematical models of the constituent reactions predict the rate of motion. Signaling pathways converging on WASp/Scar proteins regulate the activity of Arp2/3 complex, which mediates the initiation of new filaments as branches on preexisting filaments. After a brief spurt of growth, capping protein terminates the elongation of the filaments. After filaments have aged by hydrolysis of their bound ATP and dissociation of the gamma phosphate, ADF/cofilin proteins promote debranching and depolymerization. Profilin catalyzes the exchange of ADP for ATP, refilling the pool of ATP-actin monomers bound to profilin, ready for elongation.

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