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
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.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
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: 649–665
Duden R, Allan VJ, Kreis TE (1991) Involvement of 0-COP in membrane traffic through the Golgi complex. Trends Cell Biol 1: 14–19
Griffiths G, Simons K (1986) The trans Golgi network: sorting at the exit site of the Golgi complex. Science 234: 438–443.
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: 250–263
Mellman I, Simons K (1992) The Golgi complex: in vitro veritas? Cell 8: 829–840
Klausner RD, Donaldson JG, Lippincott-Schwartz J (1992) Brefeldin A: insights into the control of membrane traffic and organelle structure. J Cell Biol 116: 1071–1080
Kreis TE (1992) Regulation of vesicular and tubular membrane traffic of the Golgi complex by coat proteins. Curr Op Cell Biol, in press
Pearse BMF, Robinson MS (1990) Clathrin, adaptors, and sorting. Annu Rev Cell Biol 6: 151–171
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: 3003–3012
Rickard, J.E. and Kreis, T.E. (1990) Identification of a novel nucleotide-sensitive microtubule-binding protein in HeLa cells. J Cell Biol 110: 1623–1633
Rothman JE, Orci L (1992) Molecular dissection of the secretory pathway. Nature 355: 409–415
Scheel J, Kreis TE (1991) Motor protein independent binding of endocytic carrier vesicles to microtubules in vitro. J Biol Chem 266: 18141–18148
Schekman R (1985) Protein localization and membrane traffic in yeast. Annu Rev Cell Biol 1: 115–144
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: 185–196
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: 239–253
Waters MG, Serafini T, Rothman JE (1991) “Coatomer”: a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. Nature 349: 248–251
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1993 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Duden, R. et al. (1993). β-COP, a Coat Protein of Nonclathrin-Coated Vesicles of the Golgi Complex, is Involved in Transport of Vesicular Stomatitis Virus Glycoprotein. In: Morré, D.J., Howell, K.E., Bergeron, J.J.M. (eds) Molecular Mechanisms of Membrane Traffic. NATO ASI Series, vol 74. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-02928-2_26
Download citation
DOI: https://doi.org/10.1007/978-3-662-02928-2_26
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-662-02930-5
Online ISBN: 978-3-662-02928-2
eBook Packages: Springer Book Archive