Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments.

ABSTRACT: Members of the cofilin/ADF family of proteins sever actin filaments, increasing the number of filament ends available for polymerization or depolymerization. Cofilin binds actin filaments with positive cooperativity, forming clusters of contiguously bound cofilin along the filament lattice. Filament severing occurs preferentially at boundaries between bare and cofilin-decorated (cofilactin) segments and is biased at 1 side of a cluster. A molecular understanding of cooperative binding and filament severing has been impeded by a lack of structural data describing boundaries. Here, we apply methods for analyzing filament cryo-electron microscopy (cryo-EM) data at the single subunit level to directly investigate the structure of boundaries within partially decorated cofilactin filaments. Subn

SUBMITTER: Huehn AR 

PROVIDER: S-EPMC6983403 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature