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{"CAPTION FIG1.png": "'Figure 1: Effect of ADF/Cofilin on Different Actin Network Architectures (A) Schematic description of the experiment performed in Figure 1. (B) Left: time course of Alexa-568-labeled actin (2 \u03bcM assembly on Las-17-coated micropatterns in the presence of Arp2/3 complex (20 nM), prior to the addition of ADF/cofilin. Right: color-coded cartoon of actin network architectures. (C) Quantification of (B). Actin network normalized fluorescence intensity along the yellow linescan indicated in (B) after a 115 min polymerization time is shown. (D) Left: time course of Alexa-488-labeled ADF/cofilin (2 \u03bcM; gravel) binding to actin networks (red). Right: quantification of actin (red) and ADF/cofilin (green) fluorescence intensities, normalized to their peak intensities. Scale bars represent 30 \u03bcm. See also Figure S1 and Movie S1.\\n\\n'", "CAPTION FIG2.png": "'Figure 2: Effect of Alp1 on ADF/Cofilin-Bound Actin Networks (**A**) Schematic description of the experiment performed in Figures 2A and 2B and 2C. (**B**) Left panels: Trna course of Alp1-SAAP-Alaxa-647 (1 uM; in black) binding to ADF/cofilin-decorated actin networks. Right panels: Quantification of actin (_n_ red, Alp2/cofilin (_n_ green) and Alp1 (_n_ blue) fluorescence intensities, normalized to their peak intraclassics. Scale Bar represents 30 \u03bcm. See abs More S9.\\n\\n'", "CAPTION FIG3.png": "'Figure 3: **Quantitative Measurement of ADF/Cofflin Accumulation along the Side of Individual Actin Filaments** (A) Time course of Alexa-488-labeled ADF/cofflin (green) binding to individual actin filaments (800 nM; red), at the indicated concentrations. White arrowheads show representative examples of ADF/cofflin cooperative binding to actin filaments. Blue arrowheads show a representative example of a swerving event, where ADF/cofflin molecules remain mainly on one and of the fragments. The scale bar represents 5 \\\\(\\\\mu\\\\)m. (B) Quantification of (A). A time course of four representative molecular accumulations of ADF/cofflin along actin filaments for 180 nM (dotted lines) or 360 nM (continuous line) or ADF/cofflin is shown. Curves are plotted in blue prior to fragmentation and in red after fragmentation occurred. (C) Quantification of (A) and (B). Distribution of the number of ADF/cofflin molecules bound to actin filaments prior to sevaring is shown (23 = 11 molecules; n = 46). Error bars indicate the SD. (D) Representative field of observation after many fragmentation events with 360-_n_M ADF/cofflin. The scale bar represents 10 \\\\(\\\\mu\\\\)m. (E) Fluorescence recovery after photobleaching (FRAP) of ADF/cofflin accumulations after sevaring. (F) Time course of actin filament elongation after sevaring. The scale bar represents 5 \\\\(\\\\mu\\\\)m. (B) Kymograph of (D), plotted along the axis of the filament. See also Figures S2\u2013S4 and (A). (B). Distribution of the number of ADF/cofflin molecules bound to actin filaments prior to sevaring is shown (23 = 11 molecules; n = 46). Error bars indicate the SD.\\n\\n'", "CAPTION FIG4.png": "'Figure 4: Effect of Alp1 on Individual ADF/Cofilin-Bound Actin Filaments (A) Schematic description of the experiment performed in Figure 4.\\n\\n(B) Time course of Alp1*s (1 mM) effect on individual actin filaments (800 mM; red) decorated with various amounts of ADF/cofilin (green). White arrowheads track representative examples of ADF/cofilin stretches bound to the side of actin filaments (non-sewaving events). Red arrowheads track representative examples of ADF/cofilin stretches bound to the parload end of actin filaments (subsequent to a sawering event). Scale bars represent 5 mM.\\n\\n(C) Quantification of (B). A time course of three representative ADF/cofilin stretches along actin filaments at 180 mM (black curve) and 360 nM (red and blue curves) at ADF/cofilin after injection of Alp1 is shown. Clusters of ADF/cofilin are obscured either before (blue curve) or after (red curve) the fragmentation occurred. Fluorescence signal decrease of end-binding ADF/cofilin clusters were fitted with a microenvironmental decay (\\\\(\\\\Gamma_{\\\\text{disc}}=1.3\\\\pm 1.1\\\\); \\\\'", "CAPTION FIG5.png": "'Figure 6: **Actin Filament Elongation Assay in the Presence of ADF/Cotfillin and Alp1**(A) Time course of Alexa-558-actin filament (800 nM; red) elongation in the presence of 360 nM ADF/cotfin after injection of 800 nM Alexa-647-actin monomers (blue) and 20 nM capping protein. (B) Time course of Alexa-558-actin filament (800 nM; red) elongation in the presence of 360 nM ADF/cotfin after injection of 800 nM Alexa-647-actin monomers (blue) and 1 uM Alp1. The scale bar represents 5 um.\\n\\n'", "CAPTION FIG6.png": "'Figure 6: Effect of ADF/Cotfilin and Alp1 on Actin Filaments Blocked by Capping Protein\\n\\nTop: time course of actin filament (800 nM) elongation in the presence of 2-uM Alexa-488-ADF/cotfilin for 4 min, followed by a first injection of 20-nM capping protein for 16 min and a second injection of 1-uM Aipt. The scale bar represents 5 \u03bcm. Bottom: kymograph of the experiment plotted along the axis of an representative actin filament.\\n\\n'", "CAPTION FIG7-1.png": "'Figure 7: Models for the DIsassembly of Actin by ADF/Cofilin and Alp1 (A) Bioassembly at the whole-network scale: architecture dependence. In this model, binding of ADF/cofilin to actin cables does not trigger their disassembly, but switches actin filaments (blue filaments) to a pre-diassembly state (red filaments) (top). However, ADF/cofilin has an important effect for the dismantling of branched networks, through its de-branching activity (bottom). For all actin networks, presence of Alp1 turns these stable ADF/cofilin-decorated structures into unstable assemblies, prone to stochastic disassembly. (B) Swarming and disassembly at the single-filament scale. In this model, binding of ADF/cofilin needs to reach a threshold level of 23 molecules to trigger a conformational change of the filaments (represented by a change in their color, from blue to red). At a low concentration of ADF/cofilin (left), the threshold level is not reached. At an intermediate concentration of ADF/cofilin (center), actin filaments decorated by sub-stoichiometric densities of ADF/cofilin but with N > 23.\\n\\n'", "CAPTION FIG7-2.png": "'molecules of ADF/coffin are prone to an asymmetric swearing event. After fragmentation, ADF/coffin stretches remain near the pointed ends (PO), while barbed ends (BA) remain free to elongate. At a high concentration of ADF/coffin (right), filaments decorated by stoichiometric densities of ADF/coffin are stable. In this model, the conformation of actin filaments regulates the activity of Aip1. Only actin filaments decorated with N > 23 molecules of ADF/coffin undergo a fast stochastic disassembly.\\n\\n'", "CAPTION FIG7.png": "'* [18] J. M. C. _et al._, \"The \\\\(\\\\pi^{+}\\\\pi^{-}\\\\)'"} |
