Abstract
Synaptotagmin, a likely calcium sensor for synaptic transmission, and SNAP-25, a t-SNARE of the presynaptic plasma membrane, are key proteins for the docking and fusion of synaptic and other vesicles. We report that both synaptotagmin and SNAP-25 are palmitoylated with their fatty acids attached in a labile thioester-type bond. A SNAP-25 mutant with deleted palmitoylation sites is found exclusively in the cytosol after cell fractionation, whereas the palmitoylated form of SNAP-25 is membrane-bound, establishing that SNAP-25 is membrane-anchored via covalently linked palmitate.
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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Acylation
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Amino Acid Sequence
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Calcium-Binding Proteins*
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Cell Fractionation
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Cell Membrane / chemistry
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Cysteine / chemistry
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Cytosol / chemistry
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Membrane Glycoproteins / chemistry*
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Membrane Proteins / chemistry
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Molecular Sequence Data
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Mutation
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Nerve Tissue Proteins / analysis
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Nerve Tissue Proteins / chemistry*
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Palmitic Acid
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Palmitic Acids / chemistry*
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Qa-SNARE Proteins
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Synaptosomal-Associated Protein 25
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Synaptotagmins
Substances
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Calcium-Binding Proteins
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Membrane Glycoproteins
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Membrane Proteins
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Nerve Tissue Proteins
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Palmitic Acids
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Qa-SNARE Proteins
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Synaptosomal-Associated Protein 25
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Synaptotagmins
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Palmitic Acid
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Cysteine