Abstract
Transport of membrane proteins between intracellular compartments requires specific sequences in the protein cytoplasmic domain to direct packaging into vesicle shuttles. A sequence that mediates export from the endoplasmic reticulum (ER) has proved elusive. A di-acidic signal (Asp-X-Glu, where X represents any amino acid) on the cytoplasmic tail of vesicular stomatitis virus glycoprotein (VSV-G) and other cargo molecules was required for efficient recruitment to vesicles mediating export from the ER in baby hamster kidney cells. The existence of such a signal provides evidence that export from the ER occurs through a selective mechanism.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Acid Phosphatase / metabolism
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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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Cricetinae
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Cytoplasm / chemistry
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Endoplasmic Reticulum / metabolism*
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Golgi Apparatus / metabolism
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Membrane Glycoproteins*
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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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Mutation
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Protein Folding
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Protein Sorting Signals / chemistry
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Protein Sorting Signals / metabolism*
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Receptors, Antigen, T-Cell, alpha-beta / metabolism
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Recombinant Fusion Proteins / metabolism
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Viral Envelope Proteins / chemistry*
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Viral Envelope Proteins / metabolism*
Substances
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G protein, vesicular stomatitis virus
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Membrane Glycoproteins
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Membrane Proteins
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Protein Sorting Signals
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Receptors, Antigen, T-Cell, alpha-beta
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Recombinant Fusion Proteins
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Viral Envelope Proteins
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Acid Phosphatase