Abstract
Syntaphilin is a brain-specific syntaxin-binding partner first characterized as an inhibitor of SNARE complex formation and neurotransmitter release. Here we show that syntaphilin also binds to dynamin-1 and through this interaction inhibits dynamin-mediated endocytosis. Immunoprecipitation studies from cross-linked rat synaptosomes demonstrate that an endogenous syntaphilin-dynamin-1 complex exists independently of dynamin-1 binding to amphiphysin. Functionally, syntaphilin expression inhibits transferrin internalization in COS-7 cells. These data reveal that syntaphilin is an inhibitor of both SNARE-based fusion and dynamin-mediated endocytosis.
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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Animals
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Blotting, Western
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Brain / metabolism
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COS Cells
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Carrier Proteins / metabolism*
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Cell Line
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Dynamin I / metabolism*
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Endocytosis*
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Glutathione Transferase / metabolism
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Humans
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Immunohistochemistry
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Mass Spectrometry
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Membrane Proteins
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Models, Genetic
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Nerve Tissue Proteins / metabolism*
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Precipitin Tests
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Protein Binding
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Rats
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Recombinant Fusion Proteins / metabolism
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Synaptosomes / metabolism
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Time Factors
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Transfection
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Transferrin / metabolism
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Vesicular Transport Proteins*
Substances
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Carrier Proteins
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Membrane Proteins
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Nerve Tissue Proteins
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Recombinant Fusion Proteins
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SNPH protein, human
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Snph protein, rat
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Transferrin
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Vesicular Transport Proteins
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amphiphysin
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Glutathione Transferase
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Dynamin I