Structural organization of the dynein–dynactin complex bound to microtubules

• Published in: Nature structural & molecular biology Vol. 22; no. 4; pp. 345 - 347
• Main Authors: Chowdhury, Saikat, Ketcham, Stephanie A, Schroer, Trina A, Lander, Gabriel C
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.04.2015; Nature Publishing Group
• Subjects: 631/45/612/1228; 631/535/1258; 631/535/1258/1259; 631/80/128/1441; Animals; Biochemistry; Biological Microscopy; brief-communication; Cattle; Cellular biology; Cryoelectron Microscopy; Cytoskeleton; Dynactin Complex; Dynein; Dyneins - chemistry; Dyneins - metabolism; Electron microscopy; Eukaryotes; Life Sciences; Membrane Biology; Microtubule-Associated Proteins - chemistry; Microtubule-Associated Proteins - metabolism; Microtubules; Microtubules - chemistry; Microtubules - metabolism; Models, Molecular; Physiological aspects; Protein Structure; Proteins; Structure; United States
• ISSN: 1545-9993; 1545-9985; 1545-9985
• DOI: 10.1038/nsmb.2996

EM analyses reveal the architecture of cytoplasmic dynein in complex with dynactin and the BicD2 cargo adaptor on microtubules, showing the quaternary complex positioned for unidirectional movement and cargo recruitment. 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.