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. 2007 Dec 3;179(5):1011–1025. doi: 10.1083/jcb.200707073

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Copyright © 2007, The Rockefeller University Press

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Figure 3. — Binding of FLNa and FLNa truncates to F-actin. (A) Purified recombinant protein (0.5 or 0.05 μM) was incubated with or without 5 μM rabbit skeletal muscle actin in a polymerization buffer for 1 h at 25°C. F-actin (pellet) was separated from soluble actin (supernatant) by centrifugation. The supernatant (S) and pellet (P) fractions were diluted to equivalent volumes in SDS-PAGE sample buffer and equal volumes of each were analyzed by SDS-PAGE. The slower migrating polypeptide (arrow) is the recombinant FLNa construct. The migration of actin is indicated. (B) The amount of free and bound recombinant protein was determined by quantitative densitometric analysis from the slab gels (A) and is plotted as bound/total (%) for each of the FLNa recombinant proteins. Data are means ± SD for three separate measurements. (C) ABD deficient FLNa dimers and IgFLNa8-15+24 align F-actin into bundles. 2 μM F-actin was incubated in the absence (top left) or presence of 0.4 μM ΔABDIgFLNa1-23 (monomer: top middle) or 0.4 μM ΔABDIgFLNa1-24 (dimer: top right). Dimeric truncated molecules consisting each of 2 eight-domain monomers dimerized by repeat 24 were also incubated with F-actin (bottom). Bar, 200 nm.