RT Journal Article
SR Electronic
T1 Cryo-EM shows how dynactin recruits two dyneins for faster movement
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 183160
DO 10.1101/183160
A1 Linas Urnavicius
A1 Clinton K. Lau
A1 Mohamed M. Elshenawy
A1 Edgar Morales-Rios
A1 Carina Motz
A1 Ahmet Yildiz
A1 Andrew P. Carter
YR 2017
UL http://biorxiv.org/content/early/2017/08/31/183160.abstract
AB 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/dynactin to distinct cargos. Here we use electron microscopy (EM) and single molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased toward recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two. We find that the shift toward a double dynein complex increases both force and speed. A 3.5 Å cryo-EM 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 how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein/dynactin transport machine.