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Abstract
Cofilin/ADF proteins play key roles in the dynamics of actin. We used cryo-electron microscopy of uniformly decorated actin-cofilin filaments to show that the cofilin induced change in the filament twist is due to a unique conformation of the actin molecule unrelated to any previously observed state. The changes between the actin protomer in naked F-actin and in the actin-cofilin filament are greater than the conformational changes between G- and F-actin. Cofilin/ADF proteins efficiently depolymerize F-actin only when bound at low stoichiometry to actin filaments.
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