Dynein articles within Nature Communications

Featured

  • Article
    | Open Access

    Lis1 and Nde1/Ndel1 mediate the initiation of dynein-driven transport, but the mechanism remains unclear. Here, the authors reveal that Nde1 recruits Lis1 to autoinhibited dynein and promotes Lis1-mediated assembly of active dynein transport machinery.

    • Yuanchang Zhao
    • , Sena Oten
    •  & Ahmet Yildiz

  • Article
    | Open Access

    The dynein motor complex has a variety of important functions in both dividing and non-dividing cells. Here, Gallisà et al. describe a mode of regulation of dynein based on the phosphorylation of its adaptor BICD2 by the kinase PLK1, and how this is central for the regulation of centrosome position in G2 and M.

    • Núria Gallisà-Suñé
    • , Paula Sànchez-Fernàndez-de-Landa
    •  & Joan Roig

  • Article
    | Open Access

    Organellar transport is carefully regulated, and endolysosome localized ARL8 is important for kinesin recruitment and anterograde movement. Here, the authors show that RUFY3 and RUFY4 promote retrograde transport of endolysosomes by mediating interaction of ARL8 with dynein-dynactin.

    • Tal Keren-Kaplan
    • , Amra Sarić
    •  & Juan S. Bonifacino

  • Article
    | 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

  • Article
    | 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

  • Article
    | Open Access

    The epidermis is a multi-layered epithelium formed by the differentiation of basal cells and movement into suprabasal layers. Here the authors define a role for the desmosomal cadherin desmoglein-1 in promoting the delamination of basal cells by remodeling the actin cytoskeleton through interactions with the dynein light chain Tctex-1 and cortactin.

    • Oxana Nekrasova
    • , Robert M. Harmon
    •  & Kathleen J. Green

  • Article
    | Open Access

    A growing number of cargo-specific effector proteins are being identified that interact with both dynein and dynactin and form processive dynein-dynactin-effector complexes. Here the authors identify and characterize a conserved mechanism of interaction between dynein and unrelated effector proteins.

    • In-Gyun Lee
    • , Mara A. Olenick
    •  & Roberto Dominguez

  • Article
    | Open Access

    Dynein is a microtubule motor the motility of which is affected by the microtubule-associated protein She1. Here, the authors show that She1 alters dynein stepping behavior and increases its microtubule affinity through simultaneous interactions with the microtubule and dynein microtubule binding domain.

    • Kari H. Ecklund
    • , Tatsuya Morisaki
    •  & Steven M. Markus

  • Article
    | Open Access

    Cytoplasmic dynein 2 drives retrograde intraflagellar transport but little is known about its dynamics. Here the authors use fluorescence microscopy to track labelled dynein 2 inC. elegansat the single-molecule level and report diffusion at the ciliary base, and pausing and directional switches along the cilium.

    • Jona Mijalkovic
    • , Bram Prevo
    •  & Erwin J. G. Peterman

  • Article
    | Open Access

    Human mutations in the NDE1 gene have been associated with cortical malformations and severe microcephaly. Here, the authors show in embryonic rat brains that NDE1-depleted neural progenitors arrest at three specific cell cycle stages before mitosis, resulting in a severe decrease in neurogenesis.

    • David J. Doobin
    • , Shahrnaz Kemal
    •  & Richard B. Vallee

  • Article
    | Open Access

    Cytoplasmic dynein from the yeast S. cerevisiae behaves distinctly from mammalian dyneins, despite structural conservation. Here, Nicholas et al. identify a C-terminal domain in mammalian dynein that restricts force generation and travel distance, which, when removed, allows mammalian dynein to behave like its yeast counterpart.

    • Matthew P. Nicholas
    • , Peter Höök
    •  & Arne Gennerich

  • Article |

    Dynein is a microtubule-based motor protein, but the mechanism of how it generates force is not clear. Here, Belyy et al. use an optical trapping approach to measure force and conclude that the two dynein heads function through a unique load sharing mechanism allowing them to work against forces greater than an individual head.

    • Vladislav Belyy
    • , Nathan L Hendel
    •  & Ahmet Yildiz

  • Article |

    Unlike most processive motor proteins, the stepping motion of cytoplasmic dynein’s two linked motor domains is not precisely coordinated. Cleary et al.show that the ATPase activity of just one head is required for processive movement, and that tension on the linker gates the release of the motor from microtubules.

    • Frank B. Cleary
    • , Mark A. Dewitt
    •  & Ahmet Yildiz

  • Article
    | Open Access

    LIS1 has been shown to act as a protein ‘clutch’, which binds to dynein motor proteins and prevents microtubule detachment without affecting their ATPase activity; this causes dynein to stall. Here the authors show that the GTPase Rab6a releases LIS1 from dynein, thus reactivating the motor.

    • Masami Yamada
    • , Kanako Kumamoto
    •  & Shinji Hirotsune

Browse broader subjects

Browse Dynein across other nature.com journals