23 results found
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Sec17/Sec18 act twice, enhancing membrane fusion and then disassembling cis-SNARE complexes

    Hongki Song et al.
    Sec17 (αSNAP) and Sec18 (NSF) are shown to act twice, to promote fusion per se and to recycle SNAREs after fusion.
    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. 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
    2. Immunology and Inflammation

    Fluorescence Lifetime Imaging Microscopy reveals rerouting of SNARE trafficking driving dendritic cell activation

    Daniëlle Rianne José Verboogen et al.
    A novel microscopy-based assay shows that dendritic cells encountering pathogenic stimuli form increased complexes of specific SNARE proteins, driving release of large amounts of inflammatory cytokines.
    1. Cell Biology

    ESCRTs function directly on the lysosome membrane to downregulate ubiquitinated lysosomal membrane proteins

    Lu Zhu et al.
    The lysosome membrane is a new functional location for the ESCRTs in yeast.
    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. Biochemistry and Chemical Biology

    A distinct tethering step is vital for vacuole membrane fusion

    Michael Zick, William T Wickner
    Rigorous assays of membrane fusion show that a distinct tethering step is required for lumenal compartment mixing in a manner that extends beyond simply increasing the amount of total trans-SNARE complex.
    1. Cell Biology
    2. Neuroscience

    Multiple factors maintain assembled trans-SNARE complexes in the presence of NSF and αSNAP

    Eric A Prinslow et al.
    Biophysical analyses indicate that Munc18-1, Munc13-1, synaptotagmin-1 and complexin-1 maintain assembled trans-SNARE complexes in the presence of NSF-alphaSNAP, suggesting that they form part of the primed state of synaptic vesicles.
    1. Physics of Living Systems

    Munc18-1-regulated stage-wise SNARE assembly underlying synaptic exocytosis

    Lu Ma et al.
    The Munc18-1 protein promotes formation of the t-SNARE complex and the half-zippered SNARE complex, two rate-limiting steps of SNARE assembly, to enhance membrane fusion.

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