Cryo-EM shows how dynactin recruits two dyneins for faster movement

Linas Urnavicius, Clinton K. Lau, Mohamed M. Elshenawy, Edgar Morales-Rios, Carina Motz, Ahmet Yildiz and Andrew P. Carter ()
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Linas Urnavicius: Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue
Clinton K. Lau: Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue
Mohamed M. Elshenawy: University of California at Berkeley
Edgar Morales-Rios: CINVESTAV
Carina Motz: Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue
Ahmet Yildiz: University of California at Berkeley
Andrew P. Carter: Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue

Nature, 2018, vol. 554, issue 7691, 202-206

Abstract: Abstract Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 Å resolution cryo-electron microscopy reconstruction of a dynein tail–dynactin–BICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein–dynactin transport machine.

Date: 2018
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DOI: 10.1038/nature25462

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