Turnover of branched actin filament networks by stochastic fragmentation with ADF/cofilin |
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Authors: | Reymann Anne-Cécile Suarez Cristian Guérin Christophe Martiel Jean-Louis Staiger Christopher J Blanchoin Laurent Boujemaa-Paterski Rajaa |
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Affiliation: | Laboratoire de Physiologie Cellulaire & Végétale, Institut de Recherches en Technologies et Sciences pour le Vivant, Centre National de la Recherche Scientifique/Commissariat à l'énergie atomique et aux énergies alternatives/Institut National de la Recherche Agronomique/Université Joseph Fourier, Grenoble 38054, France. |
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Abstract: | Cell motility depends on the rapid assembly, aging, severing, and disassembly of actin filaments in spatially distinct zones. How a set of actin regulatory proteins that sustains actin-based force generation during motility work together in space and time remains poorly understood. We present our study of the distribution and dynamics of Arp2/3 complex, capping protein (CP), and actin-depolymerizing factor (ADF)/cofilin in actin "comet tails," using a minimal reconstituted system with nucleation-promoting factor (NPF)-coated beads. The Arp2/3 complex concentrates at nucleation sites near the beads as well as in the first actin shell. CP colocalizes with actin and is homogeneously distributed throughout the comet tail; it serves to constrain the spatial distribution of ATP/ADP-P(i) filament zones to areas near the bead. The association of ADF/cofilin with the actin network is therefore governed by kinetics of actin assembly, actin nucleotide state, and CP binding. A kinetic simulation accurately validates these observations. Following its binding to the actin networks, ADF/cofilin is able to break up the dense actin filament array of a comet tail. Stochastic severing by ADF/cofilin loosens the tight entanglement of actin filaments inside the comet tail and facilitates turnover through the macroscopic release of large portions of the aged actin network. |
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