Abstract
Clathrin-mediated endocytosis is initiated by the recruitment of the clathrin adaptor protein AP-2 to the plasma membrane where the membrane protein synaptotagmin is thought to act as a docking site. AP-2 also interacts with endocytic motifs present in other cargo proteins. Peptides with a tyrosine-based endocytic motif stimulated binding of AP-2 to synaptotagmin and enhanced AP-2 recruitment to the plasma membrane of neuronal and non-neuronal cells. This suggests a mechanism by which nucleation of clathrin-coated pits is stimulated by the loading of cargo proteins.
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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Adaptor Protein Complex alpha Subunits
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Adaptor Proteins, Vesicular Transport
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Animals
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Binding Sites
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CHO Cells
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Calcium-Binding Proteins*
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Cattle
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Cell Membrane / metabolism
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Clathrin / metabolism*
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Coated Pits, Cell-Membrane / metabolism*
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Cricetinae
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Endocytosis*
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Membrane Glycoproteins / chemistry
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Membrane Glycoproteins / metabolism*
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Membrane Proteins / metabolism*
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / metabolism*
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Neurons / metabolism
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Oligopeptides / chemistry
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Oligopeptides / metabolism
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Oligopeptides / pharmacology*
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Phospholipase D / metabolism
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Protein Binding
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Rats
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Recombinant Fusion Proteins / metabolism
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Synaptic Membranes / metabolism*
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Synaptotagmins
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Tyrosine / chemistry
Substances
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Adaptor Protein Complex alpha Subunits
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Adaptor Proteins, Vesicular Transport
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Calcium-Binding Proteins
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Clathrin
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Membrane Glycoproteins
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Membrane Proteins
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Nerve Tissue Proteins
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Oligopeptides
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Recombinant Fusion Proteins
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Sv2a protein, rat
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Synaptotagmins
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Tyrosine
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Phospholipase D