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American Association for the Advancement of Science, Science, 6229(347), p. 1441-1446, 2015

DOI: 10.1126/science.aaa4080

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The structure of the dynactin complex and its interaction with dynein

Journal article published in 2015 by Linas Urnavicius, Kai Zhang ORCID, Aristides G. Diamant, Carina Motz, Max A. Schlager, Minmin Yu, Nisha A. Patel, Carol V. Robinson, Andrew P. Carter ORCID
This paper is available in a repository.
This paper is available in a repository.

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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-electron microscopy to 4.0Å. Our reconstruction reveals how dynactin is built around a filament containing eight copies of the actin related protein Arp1 and one of β-actin. Capped at each end by distinct protein complexes, the length of the filament is defined by elongated peptides that emerge from the α-helical shoulder domain. A further 8.2Å 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.