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. 2019 Oct 1;10:4462. doi: 10.1038/s41467-019-12434-9

Fig. 6.

Fig. 6

Model of dynamin recruitment to forming CCVs. Model of dynamin recruitment by its PRD domain with SH3 containing proteins. (1) At early stages of CCV formation dynamin interacts with intersectin which has multiple dynamin interacting (grey) and non-interacting (white) SH3 domains. (2) In the cytosol, dynamin forms a dimer, as well as SH3 domain containing proteins such as amphiphysin. The SH3 domains of the dimer are too far apart to stabilize the interaction with the PRD via multiple binding motifs. (3) On the vesicle neck, two dimers of amphiphysin are arranged such that two SH3 domains are next to each other. This ensures high affinity of dynamin with this configuration enabling the fast recruitment of dynamin