Abstract
Endophilin/SH3p4 is a protein highly enriched in nerve terminals that binds the GTPase dynamin and the polyphosphoinositide phosphatase synaptojanin, two proteins implicated in synaptic vesicle endocytosis. We show here that antibody-mediated disruption of endophilin function in a tonically stimulated synapse leads to a block in the invagination of clathrin-coated pits adjacent to the active zone and therefore to a block of synaptic vesicle recycling. We also show that in a cell-free system, endophilin is not associated with clathrin coats and is a functional partner of dynamin. Our findings suggest that endophilin is part of a biochemical machinery that acts in trans to the clathrin coat from early stages to vesicle fission.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adaptor Proteins, Signal Transducing*
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Amino Acid Sequence
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Animals
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Antibodies / pharmacology
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Caenorhabditis elegans / genetics
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Carrier Proteins / antagonists & inhibitors
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Carrier Proteins / chemistry
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Carrier Proteins / physiology*
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Cell-Free System
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Clathrin / physiology*
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Coated Pits, Cell-Membrane / physiology*
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Dynamins
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Endocytosis*
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GTP Phosphohydrolases / physiology
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Lampreys
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Microscopy, Electron
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Molecular Sequence Data
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Rats
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Spinal Cord / chemistry
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Synapses / ultrastructure
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Synaptic Vesicles / metabolism*
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Synaptic Vesicles / ultrastructure
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src Homology Domains
Substances
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Adaptor Proteins, Signal Transducing
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Antibodies
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Carrier Proteins
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Clathrin
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GTP Phosphohydrolases
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Dynamins