Figure 2

F-BAR protein binds to WASP/N-WASP via its SH3 domain to mediate membrane dynamic changes. F-BAR proteins possess a SH3 domain which binds to closed WASP/N-WASP and mediate various membrane dynamics. The SH3 domain of F-BAR protein binds to the proline-rich region of WASP/N-WASP that mediates the protein complex formation with PIP2, CDC42, and WIP, the B region of WASP binding to PIP2 while CRIB interacts with CDC42. The formation of protein complex results in the activation of closed WASP/N-WASP, leading to actin polymerization and the formation of various membrane curvature, including endocytosis, phagocytosis, filopodium, and podosome formation. Abbreviations: Arp2/3, Actin-related protein 2/3; B region, Basic region; N-WASP, Neural Wiskott-Aldrich syndrome protein; PIP2, Phosphatidylinositol (4,5)-bisphosphate; VCA, Verprolin, cofilin, acidic; WASP, Wiskott-aldrich syndrome protein; WH1, WASP homology 1; WIP, WASP interacting protein. For other abbreviations, refer to Figure 1. The diagram model is referenced from previous publications [5].