6F1V

C terminal region of the dynein heavy chains in the dynein tail/dynactin/BICDR1 complex

Summary for 6F1V

• Entry DOI: 10.2210/pdb6f1v/pdb
• Related: 6F1T 6F1U
• EMDB information: 4168 4169 4170
• Descriptor: Cytoplasmic dynein 1 heavy chain 1 (1 entity in total)
• Functional Keywords: cryo-em, complex, motor protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 273572.19

Authors

Urnavicius, L.,Lau, C.K.,Elshenawy, M.M.,Morales-Rios, E.,Motz, C.,Yildiz, A.,Carter, A.P. (deposition date: 2017-11-23, release date: 2018-01-17, Last modification date: 2024-05-15)

Primary citation

Urnavicius, L.,Lau, C.K.,Elshenawy, M.M.,Morales-Rios, E.,Motz, C.,Yildiz, A.,Carter, A.P.
Cryo-EM shows how dynactin recruits two dyneins for faster movement.
Nature, 554:202-206, 2018

PubMed 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.

PubMed: 29420470
DOI: 10.1038/nature25462

Experimental method

ELECTRON MICROSCOPY (3.4 Å)