Conserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein.
Ontology highlight
ABSTRACT: Processive transport by the microtubule motor cytoplasmic dynein requires the regulated assembly of a dynein-dynactin-adapter complex. Interactions between dynein and dynactin were initially ascribed to the dynein intermediate chain N-terminus and the dynactin subunit p150Glued. However, recent cryo-EM structures have not resolved this interaction, questioning its importance. The intermediate chain also interacts with Nde1/Ndel1, which compete with p150Glued for binding. We reveal that the intermediate chain N-terminus is a critical evolutionarily conserved hub that interacts with dynactin and Ndel1, the latter of which recruits LIS1 to drive complex assembly. In additon to revealing that the intermediate chain N-terminus is likely bound to p150Glued in act
SUBMITTER: Okada K
PROVIDER: S-EPMC10511499 | biostudies-literature | 2023 Sep
REPOSITORIES: biostudies-literature
ACCESS DATA