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The delta subunit of AP-3 is required for efficient transport of VSV-G from the trans-Golgi network to the cell surface

Academic Article
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Overview

authors

  • Nishimura, N.
  • Plutner, H.
  • Hahn, K.
  • Balch, William E.

publication date

  • May 2002

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Vesicular stomatitis virus glycoprotein (VSV-G) is a transmembrane protein that functions as the surface coat of enveloped viral particles. We report the surprising result that VSV-G uses the tyrosine-based di-acidic motif (-YTDIE-) found in its cytoplasmic tail to recruit adaptor protein complex 3 for export from the trans-Golgi network. The same sorting code is used to recruit coat complex II to direct efficient transport from the endoplasmic reticulum to the Golgi apparatus. These results demonstrate that a single sorting sequence can interact with sequential coat machineries to direct transport through the secretory pathway. We propose that use of this compact sorting domain reflects a need for both efficient endoplasmic reticulum export and concentration of VSV-G into specialized post-trans-Golgi network secretory-lysosome type transport containers to facilitate formation of viral coats at the cell surface.

subject areas

  • Adaptor Protein Complex 3
  • Adaptor Protein Complex beta Subunits
  • Adaptor Protein Complex delta Subunits
  • Animals
  • Antigens, CD
  • Binding Sites
  • Biological Transport
  • Cell Membrane
  • Cytoplasm
  • Fibroblasts
  • HeLa Cells
  • Humans
  • Kinetics
  • Lysosome-Associated Membrane Glycoproteins
  • Membrane Glycoproteins
  • Mice
  • Mice, Inbred C57BL
  • Transcription Factors
  • Vesicular stomatitis Indiana virus
  • Viral Envelope Proteins
  • trans-Golgi Network
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Identity

PubMed Central ID

  • PMC124475

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.092150699

PubMed ID

  • 11997454
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Additional Document Info

start page

  • 6755

end page

  • 6760

volume

  • 99

issue

  • 10

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