2,464 results found
    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. 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. Cell Biology

    COPI mediates recycling of an exocytic SNARE by recognition of a ubiquitin sorting signal

    Peng Xu et al.
    COPI vesicle coat protein recognizes a ubiquitin sorting signal on an exocytic v-SNARE to mediate recycling.
    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. 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. Cell Biology

    Dilation of fusion pores by crowding of SNARE proteins

    Zhenyong Wu et al.
    A few SNARE complexes suffice to fuse membranes, but many more are needed to dilate the nascent fusion pore by molecular crowding for efficient neurotransmitter or hormone release during exocytosis.
    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.
    1. Cell Biology
    2. Structural Biology and Molecular Biophysics

    Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association

    Junyi Jiao et al.
    Sec1/Munc18-family proteins chaperone SNARE assembly via a common templating mechanism.
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    Common intermediates and kinetics, but different energetics, in the assembly of SNARE proteins

    Sylvain Zorman et al.
    The energy landscape of SNARE folding and assembly is optimized for efficient stage-wise membrane fusion.
    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.

Refine your results by:

Type
Research categories