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Fig. 3. Schematic diagram of the cortactin constructs used in this study. Cortactin features a N-terminal acidic domain (NTA) which specifically binds the Arp2/3 complex and is followed by a variable number of 37 amino acids repeats, the fourth of which binds F-actin. After an
-helix of undefined function, there is a proline-rich domain (PRD). Finally, the C-terminal is a Src-homology 3 domain (SH3) able to bind the proline-rich domain of several binding partners. The arrows indicate the positions of the mutated sites.