Fig. 2. Dynamin tubulates lipids cooperatively with the actin cytoskeleton. (A,B) Co-expression of RFP-FBP17, an F-BAR-domain-containing protein, and GFP-Dyn2 results in antagonization of formation of lipid tubules, which is relieved by disruption of the actin cytoskeleton by Latrunculin B treatment (B). (A') and (B') provide a higher magnification of the vesiculation (A') or tubulation (B') of lipids at the plasma membrane. These data demonstrate the importance of the cooperation of Dyn2 and actin in vesiculation of the membrane; adapted from Itoh et al. (Itoh et al., 2005), reprinted with permission. (C) Fluorescence image of a rat fibroblast expressing a GFP-Dyn2abK44A mutant, which results in formation of dynamin-coated lipid tubules extending inwards from the plasma membrane (Cao, H. and M.A.M., unpublished data). (D,E) Two examples of PIP2-containing membranes developing long actin cables in the presence of GTP. Long actin filament bundles form, demonstrating dynamin's ability to alter the organization of actin filaments; adapted from Schafer et al. (Schafer et al., 2002), reprinted with permission.