Abstract
Recombinant v- and t-SNARE proteins reconstituted into separate lipid bilayer vesicles assemble into SNAREpins-SNARE complexes linking two membranes. This leads to spontaneous fusion of the docked membranes at physiological temperature. Docked unfused intermediates can accumulate at lower temperatures and can fuse when brought to physiological temperature. A supply of unassembled v- and t-SNAREs is needed for these intermediates to form, but not for the fusion that follows. These data imply that SNAREpins are the minimal machinery for cellular membrane fusion.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacterial Proteins / metabolism
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Cell Membrane / chemistry
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Cell Membrane / physiology*
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DNA, Bacterial / isolation & purification
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Escherichia coli / genetics
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Intracellular Membranes / chemistry
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Intracellular Membranes / metabolism
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Lipid Bilayers / chemistry
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Lipid Bilayers / metabolism
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Membrane Proteins / genetics*
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Membrane Proteins / metabolism*
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism
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Recombinant Proteins / metabolism
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SNARE Proteins
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Vesicular Transport Proteins*
Substances
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Bacterial Proteins
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DNA, Bacterial
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Lipid Bilayers
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Membrane Proteins
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Nerve Tissue Proteins
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Recombinant Proteins
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SNARE Proteins
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Vesicular Transport Proteins