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• W2019499517 abstract "Background The close subcellular proximity of different actin filament crosslinking proteins suggests that these proteins may cooperate to organize F-actin structures to drive complex cellular functions during cell adhesion, motility and division. Here we hypothesize that α-actinin and filamin, two major F-actin crosslinking proteins that are both present in the lamella of adherent cells, display synergistic mechanical functions. Methodology/Principal Findings Using quantitative rheology, we find that combining α-actinin and filamin is much more effective at producing elastic, solid-like actin filament networks than α-actinin and filamin separately. Moreover, F-actin networks assembled in the presence of α-actinin and filamin strain-harden more readily than networks in the presence of either α-actinin or filamin. Significance These results suggest that cells combine auxiliary proteins with similar ability to crosslink filaments to generate stiff cytoskeletal structures, which are required for the production of internal propulsive forces for cell migration, and that these proteins do not have redundant mechanical functions." @default.
• W2019499517 created "2016-06-24" @default.
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• W2019499517 date "2009-02-09" @default.
• W2019499517 modified "2023-10-17" @default.
• W2019499517 title "α-Actinin and Filamin Cooperatively Enhance the Stiffness of Actin Filament Networks" @default.
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• W2019499517 doi "https://doi.org/10.1371/journal.pone.0004411" @default.
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