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Showing 1–13 of 13 results
Advanced filters: Author: Samara L. Reck-Peterson Clear advanced filters

  • Using cryo-EM, Karasmanis, Reimer, and Kendrick et al. reveal a Lis1-mediated dynein dimer, termed Chi, that serves as intermediate state in relieving dynein’s autoinhibition.

    • Eva P. Karasmanis
    • Janice M. Reimer
    • Andres E. Leschziner
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 1357-1364

  • Three independent but complementary studies by the laboratories of Markus, Reck-Peterson and Yildiz identify a key role for LIS1 in modulating localization, activity and function of dynein in cells.

    • Zaw Min Htet
    • John P. Gillies
    • Samara L. Reck-Peterson
    Research
    Nature Cell Biology
    Volume: 22, P: 518-525

  • The speed and direction of myosin and kinesin motors can be optically controlled by adding a protein domain that changes conformation in response to blue light.

    • Samara L. Reck-Peterson
    News & Views
    Nature Nanotechnology
    Volume: 9, P: 661-662

  • 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
    News & Views
    Nature Structural & Molecular Biology
    Volume: 22, P: 359-360

  • LRRK2 is one of the most commonly mutated genes in familial Parkinson’s disease. Here, the authors report a cryo-EM structure of the catalytic half of LRRK2 bound to microtubules, revealing determinants of binding that are independent of LRRK2 kinase activity.

    • David M. Snead
    • Mariusz Matyszewski
    • Samara L. Reck-Peterson
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 29, P: 1196-1207

  • The molecular motor dynein is modulated by several protein regulators, including LIS1. Here, authors use cryo-EM to show how LIS1 activates dynein by disrupting its autoinhibition and stabilizing intermediate states required to assemble the complexes that mediate transport.

    • Kendrick H. V. Nguyen
    • Eva P. Karasmanis
    • Andres E. Leschziner
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-11

  • Lis1 binding to the AAA+ ring of dynein increases the microtubule affinity and slows dynein motility. Lis1 binding to the stalk of dynein restricts the sliding of the coiled coils and slows detachment from microtubules under load.

    • Emre Kusakci
    • Zaw Min Htet
    • Ahmet Yildiz
    Research
    Nature Chemical Biology
    Volume: 20, P: 521-529

  • Using cryo-EM, Kendrick et al. reveal multiple dynein conformations during dynein’s mechanochemical cycle and Lis1 binding that represent intermediate states of dynein’s activation.

    • Agnieszka A. Kendrick
    • Kendrick H. V. Nguyen
    • Andres E. Leschziner
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 1434-1444

  • The processivity of myosins and kinesins has been well studied, but how the dynein homodimer achieves continuous motion is unknown. Two-dimensional analysis of labeled, DNA-dimerized dynein demonstrates that dynein has an unusual stepping pattern and can alternate between stochastic- and tension-based stepping to achieve processivity.

    • Weihong Qiu
    • Nathan D Derr
    • Samara L Reck-Peterson
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 193-200

  • Reimer et al. used cryo-EM and cellular assays to reveal the structural and regulatory features that distinguish LRRK1 from LRRK2, and placed these features in the context of the evolution of the LRRK family of proteins.

    • Janice M. Reimer
    • Andrea M. Dickey
    • Andres E. Leschziner
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 1735-1745

  • Molecular motors destroy a microtubule lattice as they walk on it, but it is now shown that a self-healing process incorporates new dimers in the damaged regions and prevents microtubule disassembly.

    • Sarah Triclin
    • Daisuke Inoue
    • Manuel Théry
    Research
    Nature Materials
    Volume: 20, P: 883-891

  • Cytoplasmic dynein is a minus-end-directed microtubule-based motor that transports a wide range of cargoes, including organelles, RNAs, protein complexes and viruses. How a single motor can interact with and traffic such different cargoes has been unclear. Recent studies indicate how adaptor proteins, which can both activate dynein and link it to cargo, play an important role in this process.

    • Samara L. Reck-Peterson
    • William B. Redwine
    • Andrew P. Carter
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 19, P: 382-398