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. 2013 Apr 16;104(8):1709–1719. doi: 10.1016/j.bpj.2013.01.017

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© 2013 by the Biophysical Society.

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Rapid filament elongation by mDia1 formin promotes fast network assembly at low F-actin concentrations. (A) Time course of the spontaneous assembly of 5 μM Mg-ATP-actin monomers (10% pyrene labeled) in the presence of 15 μM pfn1 and the indicated concentrations of mDia1. (B) Calculated barbed end concentration (left, red circles) and the 95% F-actin polymerization time (right, blue squares) from (A) as a function of mDia1 concentration. (C) Representative images of fluorescent (Alexa 488) phalloidin-labeling of F-actin in networks forming via a spontaneous assembly of 5 μM Mg-ATP-actin, 1.2 μM α-actinin, and 15 μM pfn1 in the presence of varying concentrations of mDia1. Polymerization is initiated at t = 0 s; scale bar = 30 μm. (D) The time to steady-state bundle density (solid circles), S(q,t) steady state (open squares), and dynamic arrest (solid diamonds) as a function of mDia1 concentration. (E) Steady-state linear bundle density as a function of mDia1 concentration. (F) Concentration of actin polymer at gelation time as a function of mDia1 concentration.