Coronin: the double-edged sword of actin dynamics

Coronin is a conserved actin binding protein that promotes cellular processes that rely on rapid remodeling of the actin cytoskeleton, including endocytosis and cell motility. However, the exact mechanism by which coronin contributes to actin dynamics has remained elusive for many years. Here, we integrate observations from many groups and propose a unified model to explain how coronin controls actin dynamics through coordinated effects on Arp2/3 complex and cofilin. At the front end of actin networks, coronin protects new (ATP-rich) filaments from premature disassembly by cofilin and recruits Arp2/3 complex to filament sides, leading to nucleation, branching and network expansion. At the rear of networks, coronin has strikingly different activities, synergizing with cofilin to dismantle old (ADP-rich) filaments. Thus, coronin spatially targets Arp2/3 complex and cofilin to opposite ends of actin networks. The net effect of coronin's activities is acceleration of polarized actin subunit flux through filamentous arrays. This increases actin network plasticity and replenishes the actin monomer pool required for new filament growth.