Structure of dynein-dynactin on microtubules shows tandem adaptor binding.

ABSTRACT: Cytoplasmic dynein is a microtubule motor that is activated by its cofactor dynactin and a coiled-coil cargo adaptor^1-3. Up to two dynein dimers can be recruited per dynactin, and interactions between them affect their combined motile behaviour^4-6. Different coiled-coil adaptors are linked to different cargos^7,8, and some share motifs known to contact sites on dynein and dynactin^4,9-13. 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 m

SUBMITTER: Chaaban S 

PROVIDER: S-EPMC7613678 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature