Significance Arp2/3 complex consists of actin-related proteins 2 and 3 with five other subunits. It forms actin filament branches under the regulation of ATP, actin monomers, actin filaments, and a nucleation-promoting factor (NPF). Here we used fluorescence spectroscopy and EM to characterize conformational changes in Arp2/3 complex along the pathway of actin filament branch formation. ATP binding to Arp2/3 complex causes small local changes in Arp2 and Arp3. NPF binding causes a larger conformational change that moves Arp2 closer to Arp3 and favors binding to the side of an actin filament, which allows further rearrangement of the subunits in the complex and growth of the new branch.
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Espinoza-Sanchez et al. (2018) studied this question.
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