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    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. Neuroscience

    A synaptotagmin suppressor screen indicates SNARE binding controls the timing and Ca2+ cooperativity of vesicle fusion

    Zhuo Guan et al.
    A suppressor screen of dominant-negative synaptotagmin-induced lethality in Drosophila identifies key properties of the protein that regulate fusion, including the SNARE interaction surface.
    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. 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. Biochemistry and Chemical Biology

    Membranes linked by trans-SNARE complexes require lipids prone to non-bilayer structure for progression to fusion

    Michael Zick et al.
    Lipids with a propensity to form nonbilayer structures must be present for the last step of membrane fusion to take place.
    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. Neuroscience

    Doc2B acts as a calcium sensor for vesicle priming requiring synaptotagmin-1, Munc13-2 and SNAREs

    Sébastien Houy et al.
    Doc2B functions in two distinct vesicle priming steps; membrane localization occludes upstream Ca2+-dependent priming, whereas Ca2+-binding and interaction with synaptotagmin-1, SNAREs, and Munc13-2 are involved in downstream priming, which makes vesicles readily releasable.
    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.
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors

    Kasper R Andersen et al.
    Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.
    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.