Advertisement

β-COP, a Coat Protein of Nonclathrin-Coated Vesicles of the Golgi Complex, is Involved in Transport of Vesicular Stomatitis Virus Glycoprotein

  • R. Duden
  • B. Storrie
  • R. Pepperkok
  • J. Scheel
  • B. Joggerst-Thomalla
  • A. Sawyer
  • H. Horstmann
  • G. Griffiths
  • T. E. Kreis
Conference paper
Part of the NATO ASI Series book series (volume 74)

Abstract

The Golgi complex is a polarized cytoplasmic organelle that is generally considered to be built up of at least three functionally distinct, membrane bounded subcompartments, the cis-Golgi network (CGN), the stacked Golgi cisternae and the trans-Golgi network (TGN) [Mellman and Simons, 1992]. It receives material from the endoplasmic reticulum (ER) and endosomes, transports cargo through its subcompartments and delivers it to the plasma membrane and endosomes. Vesicular carriers are believed to mediate the vectorial transport of this material from one membrane bounded subcompartment to the next. Recently, the idea that transport may also occur by transient tubular connections has also been discussed [Klausner et al., 1992; Kreis, 1992]; until now, however, the evidence for this mechanism of membrane transport is less convincing than for vesicular transport.

Keywords

Coat Protein Golgi Complex Coated Vesicle Vesicular Structure Membrane Traffic 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Duden R, Griffiths G, Frank R, Argos P, Kreis TE (1991) ß-COP, a 110kD protein associated with nonclathrin coated vesicles and cisternae of the Golgi complex shows homology to b-adaptin. Cell 46: 649–665CrossRefGoogle Scholar
  2. Duden R, Allan VJ, Kreis TE (1991) Involvement of 0-COP in membrane traffic through the Golgi complex. Trends Cell Biol 1: 14–19PubMedCrossRefGoogle Scholar
  3. Griffiths G, Simons K (1986) The trans Golgi network: sorting at the exit site of the Golgi complex. Science 234: 438–443.PubMedCrossRefGoogle Scholar
  4. Ho WC, Allan VJ, van Meer G, Berger EG, Kreis TE (1989) Reclustering of scattered Golgi elements occurs along microtubules. Europ J Cell Biol 48: 250–263PubMedGoogle Scholar
  5. Mellman I, Simons K (1992) The Golgi complex: in vitro veritas? Cell 8: 829–840CrossRefGoogle Scholar
  6. Klausner RD, Donaldson JG, Lippincott-Schwartz J (1992) Brefeldin A: insights into the control of membrane traffic and organelle structure. J Cell Biol 116: 1071–1080PubMedCrossRefGoogle Scholar
  7. Kreis TE (1992) Regulation of vesicular and tubular membrane traffic of the Golgi complex by coat proteins. Curr Op Cell Biol, in pressGoogle Scholar
  8. Pearse BMF, Robinson MS (1990) Clathrin, adaptors, and sorting. Annu Rev Cell Biol 6: 151–171PubMedCrossRefGoogle Scholar
  9. Pepperkok, R., Bré, M.-H., Davoust, J. and Kreis, T.E. (1990) Microtubules are stabilized in confluent epithelial cells but not in fibroblasts. J Cell Biol 111: 3003–3012PubMedCrossRefGoogle Scholar
  10. Rickard, J.E. and Kreis, T.E. (1990) Identification of a novel nucleotide-sensitive microtubule-binding protein in HeLa cells. J Cell Biol 110: 1623–1633PubMedCrossRefGoogle Scholar
  11. Rothman JE, Orci L (1992) Molecular dissection of the secretory pathway. Nature 355: 409–415PubMedCrossRefGoogle Scholar
  12. Scheel J, Kreis TE (1991) Motor protein independent binding of endocytic carrier vesicles to microtubules in vitro. J Biol Chem 266: 18141–18148PubMedGoogle Scholar
  13. Schekman R (1985) Protein localization and membrane traffic in yeast. Annu Rev Cell Biol 1: 115–144PubMedCrossRefGoogle Scholar
  14. Schweizer A, Fransen, JAM, Matter K, Kreis TE, Ginsel L, Hauri HP (1990) Identification of an intermediate compartment involved in protein transport from the endoplasmic reticulum to Golgi apparatus. Eur J Cell Biol 53: 185–196PubMedGoogle Scholar
  15. Serafini T, Orci L, Amherdt M, Brunner M, Kahn RA, Rothman JE (1991) ADP-ribosylation factor (ARF) is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell 67: 239–253PubMedCrossRefGoogle Scholar
  16. Waters MG, Serafini T, Rothman JE (1991) “Coatomer”: a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. Nature 349: 248–251Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1993

Authors and Affiliations

  • R. Duden
    • 1
  • B. Storrie
    • 1
  • R. Pepperkok
    • 1
  • J. Scheel
    • 1
  • B. Joggerst-Thomalla
    • 1
  • A. Sawyer
    • 1
  • H. Horstmann
    • 1
  • G. Griffiths
    • 1
  • T. E. Kreis
    • 1
  1. 1.European Molecular Biology LaboratoryHeidelbergGermany

Personalised recommendations