Cyclase-associated protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearly 100-fold.
CAP acts as a molecular machine that synergizes with cofilin to promote rapid actin filament depolymerization and monomer recycling.
Effect estimate: nearly 100-fold acceleration
The ability of cells to generate forces through actin filament turnover was an early adaptation in evolution. While much is known about how actin filaments grow, mechanisms of their disassembly are incompletely understood. The best-characterized actin disassembly factors are the cofilin family proteins, which increase cytoskeletal dynamics by severing actin filaments. However, the mechanism by which severed actin filaments are recycled back to monomeric form has remained enigmatic. We report that cyclase-associated-protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearly 100-fold. Structural work uncovers the molecular mechanism by which CAP interacts with actin filament pointed end to destabilize the interface between terminal actin subunits, and subsequently recycles the newly-depolymerized actin monomer for the next round of filament assembly. These findings establish CAP as a molecular machine promoting rapid actin filament depolymerization and monomer recycling, and explain why CAP is critical for actin-dependent processes in all eukaryotes.
Kotila et al. (Fri,) reported a other. Cyclase-associated protein (CAP) and cofilin vs. Bare actin filaments or absence of CAP was evaluated on Actin filament pointed end depolymerization rate (nearly 100-fold acceleration). Cyclase-associated protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearly 100-fold.