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Beta-cop is essential for transport of protein from the endoplasmic-reticulum to the golgi in-vitro

Academic Article
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Overview

authors

  • Peter, F.
  • Plutner, H.
  • Zhu, H. Y.
  • Kreis, T. E.
  • Balch, William E.

publication date

  • September 1993

journal

  • Journal of Cell Biology  Journal

abstract

  • Using a novel in vitro assay which allows us to distinguish vesicle budding from subsequent targeting and fusion steps, we provide the first biological evidence that beta-COP, a component of non-clathrin-coated vesicles believed to mediate intraGolgi transport, is essential for transport of protein from the ER to the cis-Golgi compartment. Incubation in the presence of beta-COP specific antibodies and F(ab) fragments prevents the exit of vesicular stomatitis virus glycoprotein (VSV-G) from the ER. These results demonstrate that beta-COP is required for the assembly of coat complexes mediating vesicle budding. Fractionation of rat liver cytosol revealed that a major biologically active form of beta-COP was found in a high molecular pool (> 1,000 kD) distinct from coatomer and which promoted efficient vesicle budding from the ER. Surprisingly, rab1B could be quantitatively coprecipitated with this beta-COP containing complex and was also essential for function. We suggest that beta-COP functions in an early step during vesicle formation and that rab1B may be recruited as a component of a precoat complex which participates in the export of protein from the ER via vesicular carriers.

subject areas

  • Animals
  • Antibodies
  • Antibody Specificity
  • Antigen-Antibody Complex
  • Biological Transport
  • Cell Fractionation
  • Cell Line
  • Coatomer Protein
  • Cytosol
  • Endoplasmic Reticulum
  • GTP-Binding Proteins
  • Golgi Apparatus
  • Immunoglobulin Fab Fragments
  • Liver
  • Membrane Glycoproteins
  • Microtubule-Associated Proteins
  • Precipitin Tests
  • Protein Processing, Post-Translational
  • Rats
  • Viral Envelope Proteins
  • rab1 GTP-Binding Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.122.6.1155

PubMed ID

  • 8376457
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Additional Document Info

start page

  • 1155

end page

  • 1167

volume

  • 122

issue

  • 6

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