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Showing 1–11 of 11 results
Advanced filters: Author: Kathleen M. Trybus Clear advanced filters
  • Here, Robert-Paganin et al. show that myosin A from Plasmodium falciparum is critical for red blood cell invasion and that non-canonical interactions and regulated phosphorylation are important for force generation during parasite invasion.

    • Julien Robert-Paganin
    • James P. Robblee
    • Anne Houdusse
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12
  • The fission yeast cytokinetic ring assembles by Search-Capture-Pull-Release from precursor nodes that include formin Cdc12 and myosin Myo2. The authors reconstitute Search-Capture-Pull in vitro and find that Myo2 pulling on Cdc12-associated actin filaments mechano-inhibits Cdc12-mediated assembly, which enables proper ring assembly in vivo.

    • Dennis Zimmermann
    • Kaitlin E. Homa
    • David R. Kovar
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-13
  • How a class V myosin transports mRNA is not well understood. Single-molecule reconstitution of messenger ribonucleoprotein complexes from purified proteins and a localizing mRNA in budding yeast demonstrates that the mRNA is instrumental in ensuring a stable, processive transport complex, whereas the number of localizing elements ('zip codes') influences run length and frequency.

    • Thomas E Sladewski
    • Carol S Bookwalter
    • Kathleen M Trybus
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 952-957
  • 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
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-11
  • 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
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-9
  • Myosin-V transports intracellular cargo along an actin filament, using a 'hand-over-hand' mechanism that moves it forward in 36-nm steps before dissociating. To achieve long run lengths, the stepping of the two myosin heads must be coordinated. Recent evidence favours the idea that this coordination is achieved by intramolecular strain between the heads, so that myosin prefers to pick up its trailing head first to search for a new actin-binding site, and move cargo forward on the actin.

    • Kathleen M. Trybus
    News & Views
    Nature Cell Biology
    Volume: 7, P: 854-856