Structural Basis for Microtubule Binding and Release by Dynein

Abstract

Motoring Along Dyneins are large and complex molecular motors that transport cargo along cellular microtubules and power the movement of cilia. An enigma is how microtubule binding and nucleotide hydrolysis are coordinated between sites separated by 25 nm. Redwine et al. (p. 1532 ) report an electron microscopy structure of the dynein microtubule-binding domain bound to microtubules in a high-affinity state and combined this with molecular dynamics and existing x-ray structures to provide a model for how dynein couples its affinity for microtubules with the nucleotide-bound state of the motor domain.