38 results found
    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 et al.
    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.
    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. 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. 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. Evolutionary Biology
    2. Microbiology and Infectious Disease

    Evolutionary stability of collateral sensitivity to antibiotics in the model pathogen Pseudomonas aeruginosa

    Camilo Barbosa et al.
    Evolutionary trade-offs enhance efficacy of antibiotic therapy by constraining bacterial adaptation in dependence of drug order and trade-off effect size.
    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
    2. Chromosomes and Gene Expression

    Polo-like kinase-dependent phosphorylation of the synaptonemal complex protein SYP-4 regulates double-strand break formation through a negative feedback loop.

    Saravanapriah Nadarajan et al.
    PLK-1/2-mediated SYP-4 phosphorylation is dependent on crossover precursor formation, triggering a switch in the dynamic state of the synaptonemal complex that reduces the formation of further double-strand breaks at late meiotic prophase.
    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.

Refine your results by:

Type
Research categories