7Z8I

The barbed end complex of dynactin bound to BICDR1 and the cytoplasmic dynein tails (A2, B1, B2)

Summary for 7Z8I

• Entry DOI: 10.2210/pdb7z8i/pdb
• EMDB information: 14552
• Descriptor: ARP1 actin related protein 1 homolog A, Capping protein (Actin filament) muscle Z-line, alpha 1, F-actin capping protein beta subunit, ... (9 entities in total)
• Functional Keywords: dynein, dynactin, cargo transport, activating adaptor, cytoskeleton, structural protein
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 17
• Total formula weight: 2303905.80

Authors

Chaaban, S.,Carter, A.P. (deposition date: 2022-03-17, release date: 2022-08-17, Last modification date: 2024-07-24)

Primary citation

Chaaban, S.,Carter, A.P.
Structure of dynein-dynactin on microtubules shows tandem adaptor binding.
Nature, 610:212-216, 2022

PubMed Abstract: Cytoplasmic dynein is a microtubule motor that is activated by its cofactor dynactin and a coiled-coil cargo adaptor. Up to two dynein dimers can be recruited per dynactin, and interactions between them affect their combined motile behaviour. Different coiled-coil adaptors are linked to different cargos, and some share motifs known to contact sites on dynein and dynactin. There is limited structural information on how the resulting complex interacts with microtubules and how adaptors are recruited. Here we develop a cryo-electron microscopy processing pipeline to solve the high-resolution structure of dynein-dynactin and the adaptor BICDR1 bound to microtubules. This reveals the asymmetric interactions between neighbouring dynein motor domains and how they relate to motile behaviour. We found that two adaptors occupy the complex. Both adaptors make similar interactions with the dyneins but diverge in their contacts with each other and dynactin. Our structure has implications for the stability and stoichiometry of motor recruitment by cargos.

PubMed: 36071160
DOI: 10.1038/s41586-022-05186-y

Experimental method

ELECTRON MICROSCOPY (3.3 Å)