The structure of the dynactin complex and its interaction with dynein

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Abstract

Dynactin is an essential cofactor for the microtubule motor cytoplasmic dynein-1.We report the structure of the 23-subunit dynactin complex by cryo-electronmicroscopy 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.

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Urnavicius, L., Zhang, K., Diamant, A. G., Motz, C., Schlager, M. A., Yu, M., … Carter, A. P. (2015). The structure of the dynactin complex and its interaction with dynein. Science, 347(6229), 1441–1446. https://doi.org/10.1126/science.aaa4080

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