Researchers have sought to understand the function and regulation of the motor protein dynein since its discovery more than 50 years ago1. Dynein-2 is one of the motors that move the intraflagellar transport (IFT) trains ― large protein complexes that are needed for the assembly and function of eukaryotic cilia and flagella. Toropova et al. report the single-particle cryo-EM structure of the human dynein-2 complex2, which unexpectedly reveals two different conformations of the motor subunit tails. One tail forms a zigzag that matches the periodicity of the IFT trains, which reinforces the auto-inhibition of dynein motor activity and the binding of multiple dynein-2 complexes along the train during anterograde transport.
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Dutcher, S.K. Dynein tails: how to hitch a ride on an IFT train. Nat Struct Mol Biol 26, 760–761 (2019). https://doi.org/10.1038/s41594-019-0285-z
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DOI: https://doi.org/10.1038/s41594-019-0285-z
