Abstract
Although signals for retention in the endoplasmic reticulum (ER) have been identified in the cytoplasmic domain of various ER-resident type I transmembrane proteins, the mechanisms responsible for ER retention are still unknown. Yeast and mammalian ER retention motifs interacted specifically in cell lysates with the coatomer, a polypeptide complex implicated in membrane traffic. Mutations that affect the ER retention capacity of the motifs also abolished binding of the coatomer. These results suggest a role for the coatomer in the retrieval of transmembrane proteins to the ER in both yeast and mammals.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Biological Transport
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Cell Line
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Coatomer Protein
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Endoplasmic Reticulum / metabolism*
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Fungal Proteins / chemistry
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Fungal Proteins / metabolism*
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Golgi Apparatus / metabolism
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Hexosyltransferases*
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Lysine / chemistry
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Lysine / metabolism*
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Membrane Proteins / metabolism*
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Molecular Sequence Data
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Mutation
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Transferases / chemistry
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Transferases / metabolism*
Substances
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Coatomer Protein
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Fungal Proteins
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Membrane Proteins
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Recombinant Fusion Proteins
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Transferases
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Hexosyltransferases
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dolichyl-diphosphooligosaccharide - protein glycotransferase
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Lysine