137 results found
    1. Biochemistry and Chemical Biology

    Sec17/Sec18 can support membrane fusion without help from completion of SNARE zippering

    Hongki Song et al.
    Sec18(NSF) and Sec17(αSNAP) provide a parallel pathway to fusion that is independent of energy from SNARE zippering.
    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

    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

    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

    An allosteric Sec61 inhibitor traps nascent transmembrane helices at the lateral gate

    Andrew L MacKinnon et al.
    A small molecule, cotransin, blocks transmembrane domains form integrating into cell membranes by allosterically ‘locking’ the lateral gate of the Sec61 translocation channel.
    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. Structural Biology and Molecular Biophysics

    A Sec14-like phosphatidylinositol transfer protein paralog defines a novel class of heme-binding proteins

    Danish Khan et al.
    A new class of fungal hemoproteins is described that emphasizes the versatility of the Sec14-fold for translating binding of chemically distinct ligands to control of diverse sets of cellular activities.
    1. Cell Biology

    The Sec61 translocon limits IRE1α signaling during the unfolded protein response

    Arunkumar Sundaram et al.
    Building on previous work (Plumb et al., 2015), it is shown that the Sec61 translocon controls the oligomerization, activation and inactivation of Ire1α during endoplasmic reticulum stress.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    An ER translocon for multi-pass membrane protein biogenesis

    Philip T McGilvray et al.
    A set of ER-localized membrane proteins whose loss causes developmental diseases in humans, assemble with Sec61 into a translocon that facilitates the biogenesis of hundreds of different multi-pass membrane proteins.
    1. Cell Biology

    Boundary cells restrict dystroglycan trafficking to control basement membrane sliding during tissue remodeling

    Shelly TH McClatchey et al.
    A Notch-mediated signaling pathway upregulates a Sec14-GOLD phosphopholipid binding protein that promotes a morphogenetic process important in tissue remodeling and renewal.

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