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Showing 1–15 of 15 results
Advanced filters: Author: Jenny E Hinshaw Clear advanced filters

  • Mitochondria go through cycles of fusion and fission. The yeast dynamin-related protein, Dnm1, localizes to sites of membrane fission and fusion. Hinshaw and coworkers solve the structure of Dnm1-lipid tubes by cryo-EM and compare it to dynamin. Upon GTP addition, the Dnm1-lipid tubes constrict by ~50 nm, reducing the underlying lipid membrane. This suggests that Dnm1 has the ability to impart a large contractile force during mitochondrial division.

    • Jason A Mears
    • Laura L Lackner
    • Jenny E Hinshaw
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 20-26

  • Cryo-electron tomography requires thin samples. Few cell-thinning techniques have been standardized. Here, the authors provide and validate a method to prepare, label, and image proteins at mammalian cell plasma membranes for sub-nanometer structural analysis.

    • Willy W. Sun
    • Dennis J. Michalak
    • Justin W. Taraska
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-14

  • Cryo-electron microscopy structures of OPA1, mutations of which are associated with the disease dominant optic atrophy, provide insight into how structural features of OPA1 enable this protein to mediate mitochondrial-membrane fusion and remodelling.

    • Sarah B. Nyenhuis
    • Xufeng Wu
    • Jenny E. Hinshaw
    Research
    Nature
    Volume: 620, P: 1109-1116

  • Shin et al. report the molecular mechanics of membrane budding: actin and dynamin pull membrane inward to form a Λ-shape profile; dynamin helices convert Λ- to Ω-shape by constricting Λ’s base, and then constrict Ω-profile’s pore to form a vesicle.

    • Wonchul Shin
    • Ben Zucker
    • Ling-Gang Wu
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-18

  • Despite the widespread occurrence of O-GlcNAc modifications on proteins, the specific molecular interactions of O-GlcNAc cycling enzymes remain elusive. Here, the authors use cryo-electron microscopy to resolve the structure of human O-GlcNAcase (OGA-L) as a catalytic-stalk dimer, revealing its binding to modified histone tails.

    • Sarah B. Nyenhuis
    • Agata Steenackers
    • John A. Hanover
    ResearchOpen Access
    Communications Chemistry
    Volume: 9, P: 1-15

  • A spraying-mixing approach for preparing cryo-EM grids using the Spotiton robot allows time-resolved observations of short-lived biomolecular states.

    • Venkata P. Dandey
    • William C. Budell
    • Bridget Carragher
    Research
    Nature Methods
    Volume: 17, P: 897-900

  • Endocytosis in eukaryotic cells involves numerous specialized protein complexes and lipid domains. One particularly intriguing protein is dynamin, a large GTPase that is very different from other GTPases. Now, phospholipase D has been identified as surprising regulator of dynamin's GTPase activity.

    • Jenny E. Hinshaw
    News & Views
    Nature Cell Biology
    Volume: 8, P: 432-433

  • A cryo-electron microscopy structure of human dynamin-1 demonstrates conformational changes and sheds light on the fission of membranes during endocytosis.

    • Leopold Kong
    • Kem A. Sochacki
    • Jenny E. Hinshaw
    Research
    Nature
    Volume: 560, P: 258-262

  • The GTPase dynamin provides the driving force for fission of membrane-bound vesicular structures; here, it is shown that dynamin-driven membrane fission proceeds in two mechanistically distinct stages that are separated by a metastable hemi-fission intermediate that requires GTP hydrolysis for progression to full fission.

    • Juha-Pekka Mattila
    • Anna V. Shnyrova
    • Vadim A. Frolov
    Research
    Nature
    Volume: 524, P: 109-113