3,180 results found
    1. Neuroscience
    2. Structural Biology and Molecular Biophysics

    Ca2+-dependent release of synaptotagmin-1 from the SNARE complex on phosphatidylinositol 4,5-bisphosphate-containing membranes

    Rashmi Voleti et al.
    Ca2+-free synaptotagmin-1 binds to neuronal SNARE complexes anchored on nanodiscs, and Ca2+ releases this interaction to induce tight, specific binding to PIP2-containing membranes.
    1. Microbiology and Infectious Disease

    NSF-mediated disassembly of on- and off-pathway SNARE complexes and inhibition by complexin

    Ucheor B Choi et al.
    NSF is part of a membrane trafficking quality control system that disassembles both properly formed and off-pathway SNARE complexes, and the disassembly activity may be regulated by complexin.
    1. Cell Biology
    2. Plant Biology

    ER assembly of SNARE complexes mediating formation of partitioning membrane in Arabidopsis cytokinesis

    Matthias Karnahl et al.
    SNARE proteins are delivered as complexes already from the endoplasmic reticulum along the secretory pathway to the cell division plane to mediate the formation of the partitioning membrane by vesicle fusion.
    1. Structural Biology and Molecular Biophysics
    2. Neuroscience

    Reconciling isothermal titration calorimetry analyses of interactions between complexin and truncated SNARE complexes

    Eric A Prinslow et al.
    Isothermal titration calorimetry experiments clarify apparently discrepant results described previously and show that N-terminal sequences of complexin bind to SNARE complexes containing C-terminally truncated synaptobrevin when they include the syntaxin-1 juxtamembrane region.
    1. Structural Biology and Molecular Biophysics
    2. Neuroscience

    Complexin induces a conformational change at the membrane-proximal C-terminal end of the SNARE complex

    Ucheor B Choi et al.
    Complexin can have two conformations when bound to a ternary SNARE complex, one of which induces a conformational change of the SNARE complex at the C-terminus.
    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 et al.
    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. Structural Biology and Molecular Biophysics

    Advances in X-ray free electron laser (XFEL) diffraction data processing applied to the crystal structure of the synaptotagmin-1 / SNARE complex

    Artem Y Lyubimov et al.
    Building on previous work (Uervirojnangkoorn et al., 2015), we demonstrate how improved methods for processing XFEL diffraction data enable the determination of structures from poorly diffracting crystals.
    1. Neuroscience
    2. Structural Biology and Molecular Biophysics

    Structural principles of SNARE complex recognition by the AAA+ protein NSF

    K Ian White et al.
    Electron-cryomicroscopy structures of the supercomplex of NSF, αSNAP, and neuronal SNAREs in the presence of ATP under non-hydrolyzing conditions at 3.9 Å resolution reveal interactions between the N-terminal residues of SNAP-25 and NSF.
    1. Biochemistry and Chemical Biology

    HOPS recognizes each SNARE, assembling ternary trans-complexes for rapid fusion upon engagement with the 4th SNARE

    Hongki Song et al.
    The tethering complex HOPS employs affinity for each of the 4 SNAREs to catalyze assembly of 3-SNARE intermediates, supporting an immediate burst of membrane fusion triggered by the 4th SNARE.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Sec17 (α-SNAP) and an SM-tethering complex regulate the outcome of SNARE zippering in vitro and in vivo

    Matthew L Schwartz et al.
    Sec17 is shown to have divergent effects on pre-fusion SNARE complex activity, depending on the state of SNARE zippering and HOPS, an SM-tether complex, controls the outcome of Sec17-SNARE engagement.

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