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.

Latest Research and Reviews

  • Research
    | Open Access

    Outer-arm dyneins (OADs) assemble in large arrays on the ciliary axoneme to drive rhythmic beating. Cryo-EM structures of microtubule-bound Tetrahymena thermophila OAD arrays reveal details of this complex assembly and suggest a model for its mechanism of coordinated action.

    • Qinhui Rao
    • , Long Han
    •  & Kai Zhang
  • Research
    | Open Access

    Aktary et al. identify novel roles for the dynein light chain Dynlt3 in melanosome transport, maturation, and transfer to keratinocytes. They also find that the Wnt/βcatenin signalling pathway controls Dynlt3 levels and thus also contributes to the regulation of melanocyte transport and skin pigmentation.

    • Zackie Aktary
    • , Alejandro Conde-Perez
    •  & Lionel Larue
  • Research
    | Open Access

    Axonemal dyneins are tethered to doublet microtubules inside cilia to drive ciliary beating but the mechanisms regulating their localization and function are poorly understood. Here authors report a cryo-EM reconstruction of a three-headed axonemal dynein natively bound to doublet microtubules isolated from cilia which provides a framework to understand the roles of individual subunits.

    • Travis Walton
    • , Hao Wu
    •  & Alan Brown
  • Research
    | Open Access

    Activating adaptors that link dynein to its general cofactor dynactin recruit specific cargoes and regulate dynein’s activity and processive motility in retrograde transport. Here, the authors present the crystal structures of two adaptor complexes with the dynein light intermediate chain-1 (LIC1) and show that activating adaptors can be grouped into three structural classes based on their different interactions with LIC1.

    • In-Gyun Lee
    • , Sydney E. Cason
    •  & Roberto Dominguez

News and Comment

  • 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