Control of actin dynamics by allosteric regulation of actin binding proteins.

The regulated assembly and organization of actin filaments allows the cell to construct a large diversity of actin-based structures specifically suited to a range of cellular processes. A vast array of actin regulatory proteins must work in concert to form specific actin networks within cells, and spatial and temporal requirements for actin assembly necessitate rapid regulation of protein activity. This chapter explores a common mechanism of controlling the activity of actin binding proteins: allosteric autoinhibition by interdomain head-tail interactions. Intramolecular interactions maintain these proteins in a closed conformation that masks protein domains needed to regulate actin dynamics. Autoinhibition is typically relieved by two or more ligand binding and/or posttranslational modification events that expose key protein domains. Regulation through multiple inputs permits precise temporal and spatial control of protein activity to guide actin network formation.