9DGQ

Structure of dynein-1 on microtubules

Summary for 9DGQ

• Entry DOI: 10.2210/pdb9dgq/pdb
• EMDB information: 46844
• Descriptor: Cytoplasmic dynein 1 heavy chain 1, Dynein light intermediate chain, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: dynein, microtubule, motor protein
• Biological source: Sus scrofa (pig); More
• Total number of polymer chains: 4
• Total formula weight: 1177875.59

Authors

Rao, Q.,Chai, P.,Zhang, K. (deposition date: 2024-09-03, release date: 2025-09-10, Last modification date: 2025-10-29)

Primary citation

Rao, Q.,Chai, P.,Zhang, K.
Molecular basis for the assembly of the dynein transport machinery on microtubules.
Biorxiv, 2024

PubMed Abstract: Cytoplasmic dynein-1, a microtubule-based motor protein, requires dynactin and an adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The role of microtubules in DDA assembly has been elusive. Here, we reveal detailed structural insights into microtubule-mediated DDA assembly using cryo-electron microscopy. We find that an adaptor-independent dynein-dynactin complex (DD) predominantly forms on microtubules in an intrinsic 2:1 stoichiometry, induced by spontaneous parallelization of dynein upon microtubule binding. Adaptors can squeeze in and exchange within the assembled microtubule-bound DD complex, which is enabled by relative rotations between dynein and dynactin, and further facilitated by dynein light intermediate chains that assist in an adaptor 'search' mechanism. Our findings elucidate the dynamic adaptability of the dynein transport machinery, and reveal a new mode for assembly of the motile complex.

PubMed: 39803430
DOI: 10.1101/2024.12.30.630772

Experimental method

ELECTRON MICROSCOPY (11 Å)