Structural organization of the dynein-dynactin complex bound to microtubules.
Cytoplasmic dynein associates with dynactin to drive cargo movement on microtubules, but the structure of the dynein-dynactin complex is unknown. Using electron microscopy, we determined the organization of native bovine dynein, dynactin and the dynein-dynactin-microtubule quaternary complex. In the microtubule-bound complex, the dynein motor domains are positioned for processive unidirectional movement, and the cargo-binding domains of both dynein and dynactin are accessible.
Department of Integrative Structural and Computational Biology, Scripps Research Institute, La Jolla, California, USA.
Saikat
S
Chowdhury
Department of Biology, Johns Hopkins University, Baltimore, Maryland, USA.
Stephanie A
SA
Ketcham
Department of Biology, Johns Hopkins University, Baltimore, Maryland, USA.
Trina A
TA
Schroer
Department of Integrative Structural and Computational Biology, Scripps Research Institute, La Jolla, California, USA.
Gabriel C
GC
Lander
D000818:Animals; D002417:Cattle; D020285:Cryoelectron Microscopy; D000072159:Dynactin Complex; D004398:Dyneins / Q000737:chemistry* / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000737:chemistry* / Q000378:metabolism; D008870:Microtubules / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular
D000072159:Dynactin Complex; D008869:Microtubule-Associated Proteins; D004398:Dyneins