Dynein is a minus-end-directed microtubule motor protein, which transports a variety of intracellular cargo by hydrolysing ATP to power its movement along microtubule tracks. Axonemal dyneins are found cilia and flagella, whereas cytoplasmic dynein is found in all animal cells.

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  • News & Views |

    Active transport along microtubules by molecular motors is a crucial cellular process that is disrupted in human diseases. Single-molecule studies from three independent groups reveal a new molecular mechanism for how cells control the activity of the complex microtubule motor cytoplasmic dynein via the neurodevelopmental protein LIS1.

    • Richard J. McKenney
    Nature Cell Biology 22, 515-517
  • News & Views |

    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.

    • Susan K. Dutcher
  • News & Views |

    Dynactin is an essential cofactor for the microtubule-based motor cytoplasmic dynein. Two recent papers report structures obtained by cryo-EM of dynactin, the dynein–dynactin complex and dynein–dynactin bound to its track, the microtubule.

    • Samara L Reck-Peterson
  • Research Highlights |

    Control of the activity of the microtubule motor cytoplasmic dynein 1 is essential for its function in intracellular transport. A recent paper by McKenney et al. published in Science shows that activation of processive dynein motility requires the formation of cargo adaptor-dynein-dynactin complexes.

    • Mark P Dodding
    Cell Research 24, 1385-1386