The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.
Cryo-EM shows how dynactin recruits two dyneins for faster movement
Open accessAbstract
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.
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Metadata
- Authors
- Urnavicius, L., Lau, C. K., Elshenawy, M. M., Morales-Rios, E., Motz, C., Yildiz, A., & Carter, A. P.
- Venue
- Nature
- Published
- 2018-02
- Volume
- 554
- Issue
- 7691
- Pages
- 202-206
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2752663558
- Cited by
- 283
- References
- 65
- FWCI
- 17.32
- Type
- journal article
- Language
- en
- Open access
- green
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- Urnavicius, L., Lau, C. K., Elshenawy, M. M., Morales-Rios, E., Motz, C., Yildiz, A., & Carter, A. P. (2018). Cryo-EM shows how dynactin recruits two dyneins for faster movement. Nature. https://doi.org/10.1038/nature25462
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