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    1. Biochemistry and Chemical Biology

    Sec17/Sec18 can support membrane fusion without help from completion of SNARE zippering

    Hongki Song, Thomas L Torng ... William T Wickner
    Sec18(NSF) and Sec17(αSNAP) provide a parallel pathway to fusion that is independent of energy from SNARE zippering.
    1. Cell Biology

    High-resolution secretory timeline from vesicle formation at the Golgi to fusion at the plasma membrane in S. cerevisiae

    Robert M Gingras, Abigail M Sulpizio ... Anthony Bretscher
    The first quantitative live-cell microscopy this work shows depicting the order of events preceding secretion in budding yeast.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Membrane Fusion: To protect or reject

    Mary Munson
    Version of Record
    Insight
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18

    Braden T Lobingier, Daniel P Nickerson ... Alexey J Merz
    Sec1/Munc18 (SM) proteins shield SNARE complexes from NSF/Sec18-mediated disassembly through cooperative binding interactions with SNARE complexes and the universal co-chaperone α-SNAP/Sec17.
    1. Cell Biology
    2. Structural Biology and Molecular Biophysics

    Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association

    Junyi Jiao, Mengze He ... Yongli Zhang
    Sec1/Munc18-family proteins chaperone SNARE assembly via a common templating mechanism.
    1. Cell Biology
    2. Structural Biology and Molecular Biophysics

    The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation

    Travis J Eisemann, Frederick Allen ... Frederick M Hughson
    Whereas in a paradigmatic structure an SM protein chaperone clamps its client SNARE shut, a second structure demonstrates that an SM protein can also hold its SNARE open to promote assembly.
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