| Structural highlights
Function
ACTZ_PIG Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
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 A 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.
Cryo-EM shows how dynactin recruits two dyneins for faster movement.,Urnavicius L, Lau CK, Elshenawy MM, Morales-Rios E, Motz C, Yildiz A, Carter AP Nature. 2018 Feb 7;554(7691):202-206. doi: 10.1038/nature25462. PMID:29420470[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Urnavicius L, Zhang K, Diamant AG, Motz C, Schlager MA, Yu M, Patel NA, Robinson CV, Carter AP. The structure of the dynactin complex and its interaction with dynein. Science. 2015 Mar 27;347(6229):1441-6. doi: 10.1126/science.aaa4080. Epub 2015, Feb 12. PMID:25814576 doi:http://dx.doi.org/10.1126/science.aaa4080
- ↑ Zhang K, Foster HE, Rondelet A, Lacey SE, Bahi-Buisson N, Bird AW, Carter AP. Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated. Cell. 2017 Jun 15;169(7):1303-1314.e18. doi: 10.1016/j.cell.2017.05.025. Epub, 2017 Jun 8. PMID:28602352 doi:http://dx.doi.org/10.1016/j.cell.2017.05.025
- ↑ Urnavicius L, Lau CK, Elshenawy MM, Morales-Rios E, Motz C, Yildiz A, Carter AP. Cryo-EM shows how dynactin recruits two dyneins for faster movement. Nature. 2018 Feb 7;554(7691):202-206. doi: 10.1038/nature25462. PMID:29420470 doi:http://dx.doi.org/10.1038/nature25462
- ↑ Lau CK, O'Reilly FJ, Santhanam B, Lacey SE, Rappsilber J, Carter AP. Cryo-EM reveals the complex architecture of dynactin's shoulder region and pointed end. EMBO J. 2021 Apr 15;40(8):e106164. PMID:33734450 doi:10.15252/embj.2020106164
- ↑ Chaaban S, Carter AP. Structure of dynein-dynactin on microtubules shows tandem adaptor binding. Nature. 2022 Sep 7. pii: 10.1038/s41586-022-05186-y. doi:, 10.1038/s41586-022-05186-y. PMID:36071160 doi:http://dx.doi.org/10.1038/s41586-022-05186-y
- ↑ Urnavicius L, Lau CK, Elshenawy MM, Morales-Rios E, Motz C, Yildiz A, Carter AP. Cryo-EM shows how dynactin recruits two dyneins for faster movement. Nature. 2018 Feb 7;554(7691):202-206. doi: 10.1038/nature25462. PMID:29420470 doi:http://dx.doi.org/10.1038/nature25462
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