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Dynactin is an essential cofactor for the microtubule motor cytoplasmic dynein-1. We report the structure of the 23-subunit dynactin complex by cryo-electron microscopy to 4.0 angstroms. Our reconstruction reveals how dynactin is built around a filament containing eight copies of the actin-related protein Arp1 and one of β-actin. The filament is capped at each end by distinct protein complexes, and its length is defined by elongated peptides that emerge from the α-helical shoulder domain. A further 8.2 angstrom structure of the complex between dynein, dynactin, and the motility-inducing cargo adaptor Bicaudal-D2 shows how the translational symmetry of the dynein tail matches that of the dynactin filament. The Bicaudal-D2 coiled coil runs between dynein and dynactin to stabilize the mutually dependent interactions between all three components.

Original publication




Journal article



Publication Date





1441 - 1446


Actins, Animals, Cryoelectron Microscopy, Dynactin Complex, Dyneins, Humans, Mice, Microtubule-Associated Proteins, Multiprotein Complexes, Protein Interaction Mapping, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Subunits, Swine