Motor protein function articles within Nature Communications

Featured

  • Article
    | Open Access

    Myosin transduces chemical energy into mechanical work, but the mechanism remains unclear. In this work, the authors show that force-generation precedes product release and that a mutation in the active site alters the load dependence of product release.

    • Christopher Marang
    • , Brent Scott
    •  & Edward P. Debold

  • Article
    | Open Access

    Release of the ATP hydrolysis product orthophosphate (Pi) from the myosin active site is central in force generation but is poorly understood. Here, Moretto et al. present evidence for multistep Pi-release reconciling apparently contradictory results.

    • Luisa Moretto
    • , Marko Ušaj
    •  & Alf Månsson

  • Article
    | Open Access

    It is unclear how bacterial cells adapt the reversible switching of flagellar motor rotation to environments of different viscosities. Here, Antani et al. show that flagellar mechanosensors allosterically control the motor’s binding affinity for the chemotaxis response regulator, CheY-P, to adapt flagellar switching over varying viscous loads.

    • Jyot D. Antani
    • , Rachit Gupta
    •  & Pushkar P. Lele

  • Article
    | Open Access

    Plasmodium falciparum moves by an atypical process called gliding motility which comprises of atypical myosin A (PfMyoA) and filaments of the dynamic and divergent PfActin-1 (PfAct1). Here authors present the cryo-EM structure of PfMyoA bound to filamentous PfAct1 stabilized with jasplakinolide and provide insights into the interactions that are required for the parasite to produce the force and motion required for infectivity.

    • Julien Robert-Paganin
    • , Xiao-Ping Xu
    •  & Dorit Hanein

  • Article
    | Open Access

    Former evidence suggests a correlation between the function of non-conventional myosin motors and actin dynamics. Here authors use in vitro assays in which they observe that actin sliding on myosin 1b immobilized or bound to a fluid bilayer enhances actin depolymerization at the barbed end.

    • Julien Pernier
    • , Remy Kusters
    •  & Evelyne Coudrier

  • Article
    | Open Access

    Myosin, a motor protein essential for intracellular transport to muscle contraction, requires a chaperone UNC-45 for folding and assembly. Here authors use in vitro reconstitution and structural biology to characterize the interplay between UNC-45 and muscle myosin MHC-B.

    • Doris Hellerschmied
    • , Anita Lehner
    •  & Tim Clausen

  • Article
    | Open Access

    During cell division, it is currently unclear how kinetochores transit from lateral microtubule attachment to durable association to dynamic microtubule plus ends. Here, using in vitro reconstitution and computer modeling, the authors provide biophysical mechanism for microtubule end-conversion driven by two kinetochore components, CENP-E and Ndc80 complex

    • Manas Chakraborty
    • , Ekaterina V. Tarasovetc
    •  & Ekaterina L. Grishchuk

  • Article
    | Open Access

    Thrombospondin-1 (THSB1) is a component of the ECM with a role in regulating cancer development and tumour vasculature. Here, the authors show that TGF-beta-induced THBS1 expression contributes to the invasive behaviour of GBM cells and promotes resistance to antiangiogenic therapy partially through interaction with CD47.

    • Thomas Daubon
    • , Céline Léon
    •  & Andréas Bikfalvi

  • Article
    | Open Access

    Dynein plays roles in vesicular, organelle, chromosomal and nuclear transport but so far it is unclear how dynein activity in cells is regulated. Here authors study several dynein cofactors and their role in force adaptation of dynein during lipid droplet, lysosomal, and mitochondrial transport.

    • Dail E. Chapman
    • , Babu J. N. Reddy
    •  & Steven P. Gross

  • Article
    | Open Access

    Myosin-5B is an actin-based motor important for endosome recycling, but the molecular mechanism underlying its motility remains unknown. Here authors use single molecule imaging and high-speed laser tweezers to dissect the mechanoenzymatic properties of myosin-5B, which shows processive motility with peculiar mechanosensitivity.

    • Lucia Gardini
    • , Sarah M. Heissler
    •  & Marco Capitanio

  • Article
    | Open Access

    Kinesin-14s, such as Ncd, interact with microtubules with their non-processive motor domains and their diffusive tail domains, but the influence of the tail domains on motor performance is not known. Here the authors show that tail domain slippage limits the velocities and forces generated by Ncd, suggesting it acts as a slippery crosslinker.

    • Annemarie Lüdecke
    • , Anja-Maria Seidel
    •  & Stefan Diez

  • Article
    | Open Access

    Cellular cargo transported along actin filaments is faced with a directional choice at an intersection. Here the authors show that myosin Va-bound cargo prefers to go straight through the intersection, and propose a model to explain this by a tug-of-war between motors on the lipid cargo that engage the actin tracks.

    • Andrew T. Lombardo
    • , Shane R. Nelson
    •  & David M. Warshaw

  • Article
    | Open Access

    Myosin X is a molecular motor unique in its ability to generate filopodia, but the mechanism explaining this behaviour is not known. Here, through a combination of structure, single-molecule assays and modelling the authors show that myosin X is optimized for transport along actin bundles.

    • Virginie Ropars
    • , Zhaohui Yang
    •  & Anne Houdusse

  • Article
    | Open Access

    Centralspindlin consists of dimeric kinesin-6 and dimeric RacGAP, and is involved in the organization of anaphase midzone microtubules. Here, the authors show that the RacGAP is needed for motor activity at the plus-end of microtubules, but not for the bundling activity associated with kinesin-6.

    • Li Tao
    • , Barbara Fasulo
    •  & William Sullivan

  • Article
    | Open Access

    F1-ATPase is a rotary motor protein that can efficiently convert chemical energy of ATP hydrolysis to mechanical work. Here, the authors study its catalytic reactions using high-speed single-molecule observations and contemporary time series analysis, and propose a lock and key type mechanism.

    • Chun-Biu Li
    • , Hiroshi Ueno
    •  & Tamiki Komatsuzaki

  • Article |

    Alignment of chromosomes at the spindle equator involves two kinesin family molecular motors, Kid and CENP-E. Here, Iemura and Tanaka show differential contributions of these motors, whereby Kid promotes partial alignment before end-on microtubule attachment to chromosomes, and CENP-E promotes alignment when microtubules are stabilized.

    • Kenji Iemura
    •  & Kozo Tanaka

  • 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 |

    Vesicle trafficking in the cell is likely to involve a tug-of-war between motor proteins of opposing directionality. Guet al. use high-speed single-particle tracking in neurons to uncover rotation of paused cargo vesicles, providing insight into the changing forces as the vesicles change direction.

    • Yan Gu
    • , Wei Sun
    •  & Ning Fang

Browse broader subjects

Browse Motor protein function across other nature.com journals