Abstract
Several independent lines of evidence suggest that the traffic between the ER and the Golgi complex involves other membrane-bound structure that may form distinct compartment(s). These structures have been variously named, but their morphology has yet to be defined, and the mechanism of the transport between the ER and Golgi complex is still largely unknown. To address an aspect of this problem we used G glycoprotein synthesized by the VSV is-045 mutant strain. At the non-permissive temperature (39 °C) G glycoprotein accumulates in the ER as a multimeric aggregate and there is very little export. When the temperature is lowered to 31 °C, the aggregated protein trimerizes, leaves the ER and reachs the Golgi complex; if the temperature is lowered to 15 °C, the protein correctly trimerizes but it is arrested in an intermediate location before reaching the Golgi complex. Here we describe the morphology of this intermediate structure and the transfer of G glycoprotein from this compartment to the Golgi complex.
Keywords
- Golgi Complex
- Vesicular Stomatitis Virus
- Immunocytochemical Analysis
- Intermediate Structure
- Rab2 Protein
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.
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Lotti L V, Torrisi M R, Pascale M C, and Bonatti S (1992) J Cell Biol 118: in the press.
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© 1993 Springer-Verlag Berlin Heidelberg
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Bonatti, S., Lotti, L.V., Torrisi, M.R., Pascale, M.C. (1993). Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex. 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_5
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DOI: https://doi.org/10.1007/978-3-662-02928-2_5
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-662-02930-5
Online ISBN: 978-3-662-02928-2
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