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The actin cytoskeleton is composed of multiple networks which are specializedfor several processes such as cell motility or cell division. Each of thesenetworks are composed of organized actin microfilaments which are decoratedwith specific sets of actin binding proteins (ABPs). The molecular mechanismsguiding ABPs to specific actin networks are still poorly understood, butcooperativity, the mechanism by which the binding of an ABP is positivelyinfluenced by proximal bound ABPs, plays a crucial role in generating locallydense stretches of ABPs. Cooperative binding is characterized by its amplitude,but also by the range at which its effects are propagated along an actinfilament through long-range allosteric interactions. The range of theseallosteric effects is still debated, but is likely to be significant at thelengthscale of actin filaments in cells. Here, we investigated howcooperativity influences the clustering of ABPs, using a stochasticcomputational model of binding of ABPs to actin filaments. The model reproducesthe formation of ABP clusters observed experimentally at the single filamentscale, and provides a theoretical estimation of the range of cooperativity forproteins such as ADF/cofilin. We found that both the amplitude and the spatialrange of cooperativity dramatically impact the properties of clustering.However, the parameters of cooperativity modulate differently the rate ofassembly, size and dynamics of the ABP clusters, suggesting that cooperativityis an efficient mechanism to regulate precisely the recruitment of ABPs incells. This work provides a more general framework for future understanding ofhow actin networks acquire distinct and specific protein compositions from acommon cytoplasm.

The Range of Cooperativity Modulates Actin Binding Protein Cluster Size, Density and Dynamics