Abstract
Tyrosine-based signals within the cytoplasmic domain of integral membrane proteins mediate clathrin-dependent protein sorting in the endocytic and secretory pathways. A yeast two-hybrid system was used to identify proteins that bind to tyrosine-based signals. The medium chains (mu 1 and mu 2) of two clathrin-associated protein complexes (AP-1 and AP-2, respectively) specifically interacted with tyrosine-based signals of several integral membrane proteins. The interaction was confirmed by in vitro binding assays. Thus, it is likely that the medium chains serve as signal-binding components of the clathrin-dependent sorting machinery.
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 Proteins, Vesicular Transport
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Amino Acid Sequence
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Cell Membrane / metabolism
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Clathrin / metabolism*
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Cloning, Molecular
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Glutathione Transferase / metabolism
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Golgi Apparatus / metabolism
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Lysosomes / metabolism
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism*
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Molecular Sequence Data
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / metabolism*
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Phosphoproteins / chemistry
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Phosphoproteins / metabolism*
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Protein Sorting Signals / chemistry
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Protein Sorting Signals / metabolism*
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Recombinant Fusion Proteins / metabolism
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism
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Transformation, Genetic
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Tyrosine / metabolism*
Substances
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Adaptor Proteins, Vesicular Transport
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Clathrin
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Membrane Proteins
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Nerve Tissue Proteins
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Phosphoproteins
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Protein Sorting Signals
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Recombinant Fusion Proteins
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Tyrosine
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Glutathione Transferase