Essential Function of Dynamin in the Invasive Properties and Actin Architecture of v-Src Induced Podosomes/Invadosomes (original) (raw)
Figure 1
Dynamin is dynamically associated with actin reorganization and extracellular matrix degradation activity of invadosome rosettes.
A) Extracted images from time serie (min) from representative observations of SKO-v-Src-MEFs expressing Dyn2-pTRFP and spread on gelatin-OregonGreen degradable surface. As shown in the zoom corresponding to the red square, dyn2-pTRFP is localized in rosette (red dash circle), and is present all along the degradative activity of the structure. B–C) Extracted images from time serie (min∶s) from representative observations of SKO-v-Src-MEFs expressing Dyn2-pTRFP in association with GFP-actin and GFP-cortactin. The dynamic of invadosome ring is based on a treadmilling movememnt based on the polymerization of new actin structures at the outer rim and depolymerization of older actin structures at the inner rim of the ring. Dyn2-pTRFP is perfectly colocalized with GFP-actin and GFP-cortactin during expansion of the invadosome ring. D) Zoom on invadosome ring expansion. Quantification of fluorescence intensity (8bits color image coded from 0 to 255 levels) of Dyn2-pTRFP and GFP-actin or GFP-paxillin allowed generating the intensity profile intensity along the yellow line (24 px) in the merged image. Dyn2-pTRFP colocalized either with GFP-actin either with GFP-paxillin present also at the region of actin depolymerization (inner rim). Scale bar = 5 µm (A), 3 µm (B, C) and 0,5 µm (D).