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The Core Architecture of the WAVE Inhibitory Complex

Arp2/3 dependent control of actin polymerization at the leading edge of cellular protrusions is known to be positively regulated by the WASP/WAVE family of proteins, through a conserved domain, the VCA domain. WAVE exists as a member of a multisubunit complex of WAVE, Abi, HSPC300, NAP1 and CYFIP. The connection and importance of these proteins have been shown clearly in genetic experiments and in biochemical purifications. Yet the detailed function and architecture of this complex is still unclear. Here we present the reconstitution and characterization of two important sub complexes, using minimized protein fragments. The first is an α‐helix rich hetereotrimer composed of the N‐terminus of Abi2, the N‐terminus of WAVE1 and HSPC300. This complex is thermally stable, protease resistant and copurifies through multiple chromatography steps. The second is a purified subcomplex of an otherwise unfolded internal fragment of Abi2, and NAP1. Through this work we show that the WAVE/HSPC/Abi interface and the Abi/NAP1 interface are mediated by distinct structural units, and are connected to each other through the covalent structure of Abi2.