Interestingly, the CHMP4B-coated GUVs keep a deformed shape after being released for the micropipette (Figure 5-50 / C), suggesting that the membrane acquires a plastic behaviour when CHMP4 ,
This result is again in agreement with Chiaruttini et al. results showing a Snf7-coated GUV plastic behaviour after micropipette aspiration release ,
, FIGURE 5-50: IMAGES OF ASPIRATION EXPERIMENTS ON CHMP2B AND CHMP4B BOUND TO GUVS
, Micropipette aspiration of a GUV incubated with CHMP2B-?C (green) at different aspiration pressures: zero (top), medium (middle, ? = 0.4 mN/m) and maximum (bottom, ? = 0.6 mN/m). The corresponding image of the lipids (magenta) is shown
, Micropipette aspiration of a GUV incubated with CHMP4B polymer (cyan)
, Single confocal plane images of a GUV incubated with CHMP4B polymer (cyan) after aspiration release. Scale bar = 10 µm
, Moreover, micropipette aspiration assays on vesicles covered with CHMP4B polymer proved that
, / A shows that the stretching modulus of vesicles without proteins (magenta) and CHMP4-GUVs (blue
, Importantly, when we checked the effect of addition of CHMP2B to CHMP4B (green), we observed a stiffening of the overall structure (Figure 5-51 / B). The modulus signifies that the pre-existing CHMP4 polymer can also be rigidified by CHMP2B polymer, but conversely
, FIGURE 5-52: FRAP EXPERIMENTS ON CHMP4B VERSUS CHMP2B PROTEINS BOUND TO GUVS FRAP experiments on vesicles covered either with CHMP2B-?C or CHMP4B
, Confocal images showing fluorescence recovery for CHMP2B-?C and CHMP4B protein polymers after photobleaching. Yellow squares indicate the photobleached ROIs. White arrow shows the loss of fluorescence in an unbleached area of the GUV
, Recovery versus time after photo-bleaching of CHMP2B-?C and CHMP4B polymers. n=45 5.5.2 CHMP2B DISORGANIZES CHMP4B SPIRALS ON FLAT SURFACES We incubated CHMP4B-covered LUVs with CHMP2B and imaged the effect of the addition of CHMP2B by Cryo-EM. We observed a noticeable change in the arrangement of CHMP4B filaments, pp.5-53
, On flat deformable LUVs, CHMP4B/CHMP2B spirals appear enlarged, with increased spacing between filaments. On average, the spacing between filaments within the spirals is larger than for CHMP4B alone: a mean value
We first formed CHMP4 spirals on the SLB then added CHMP2B proteins. With HS-AFM, we could follow the changes live. A reorganization of the spiral is observed when CHMP2B is added on SLB membrane bound CHMP4B (Figure 5-53 / B). CHMP4B spirals are locally disrupted, with some filaments pushed away and other compressed; the spirals thus become very irregular (Figure 5-53), we also observed perturbations of the CHMP4B spirals on the membrane-coated mica support ,
, FIGURE 5-53: EFFECT OF CHMP2B ON CHMP4B POLYMERIZATION ON MEMBRANE
, Cryo-EM image showing the modulation of CHMP4B spirals on LUV membrane by addition of CHMP2B. Scale bar = 100 nm. Quantification of interfilament distance is shown on the right
, AFM image showing the modulation of CHMP4B spirals on SLB membrane by addition of CHMP2B. Scale bar = 100 nm
, Profiles of sections of the spiral shown in (B) between deformed filaments (green), between filaments far from the "holes
, Histograms showing different distances between distorted/deformed filaments (i.e. diameter of the holes) (green), the peak to peak between filaments far from perturbance (red) and the
, FIGURE 5-57: COMPARISON OF CHMP4B SPIRAL MEASUREMENTS IN PRESENCE OF CHMP2A/B PROTEINS (A) Schema illustrating the 3D helix parameters quantified from Cryo-EM data
, Quantification of spiral length from Cryo-EM data
Tukey's multiple comparison test) ,
, Quantification of spiral width from Cryo-EM data. (Tukey's multiple comparison test)
, Quantification of helix periodicity from Cryo-EM data. (Tukey's multiple comparison test)
, Quantification of the interfilament spacing from Cryo-EM data. (Tukey's multiple comparison test)
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