The Intermediate Compartment between Endoplasmic Reticulum and Golgi Complex in Mammalian Cells
Several lines of evidence strongly support the view that the traffic between ER and Golgi complex involves one (or more) previously unidentified membranous structure. This fascinating new finding is based on data obtained in several different experimental systems with different methodology. Unavoidably, many terms have been suggested for this structure: pre-Golgi vacuoles (Saraste and Kuismanen, 1984), budding compartment (Tooze et al., 1988), intermediate compartment (Schweizer et al., 1990), intermediate elements (Saraste and Svensson, 1991), salvage compartment (Munro and Pelham, 1987), cis-Golgi network (Mellman and Simons, 1992). Throughout this review, we will use only the term “intermediate compartment.” Many different findings and opinions on the structure and function of the intermediate compartment have been reported and will be considered throughout this review: thus, we will present our own view from the beginning, to give the readers a guideline in this intricate pathway.
KeywordsInfluenza Oligomerization Compaction Disulfide Gallione
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- Chin, D. J., Luskey, K. L., Anderson, R. G. W., Faust, J. R., Goldstein, J. L., and Brown, M. S., 1982, Appearance of crystalloid endoplasmic reticulum in compactin-resistant Chinese hamster cells with a 500-fold increase in 3-hydroxy-3-methylglutaryl-coenzyme A reductase, Proc. Natl. Acad. Sci. USA 79:1185–1189.PubMedCrossRefGoogle Scholar
- Lippincott-Schwartz, J., Donaldson, J. G., Schweizer, A., Berger, E. G., Hauri, H. P., Yuan, L. C., and Klausner, R. D., 1990, Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway, Cell 60:821–836.PubMedCrossRefGoogle Scholar
- Nasciutti, L. E., Picart, R., Rosenbaum, E., Tixier-Vidal, A., and Tougard, C., 1992, Effect of reduced temperatures and brefeldin A on prolactin secretion and on subcellular distribution of the secretory product and membrane antigens in GH3 pituitary cells, Biol. Cell 72:25–35.CrossRefGoogle Scholar
- Nguyen Van, P., Peter, F., and Soling, H. D., 1989, Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium. No indication for calsequestrinlike proteins in inositol 1,4,5-trisphosphate-sensitive calcium sequestering rat liver vesicles, J. Biol. Chem. 264:17494–17501.Google Scholar
- Pascale, M. C., Erra, M. C., Malagolini, N., Serafini-Cessi, F., Leone, A., and Bonatti, S., 1992, Post-translational processing of an O-glycosylated protein, the human CD8 glycoprotein, during the intracellular transport pathway to the plasma membrane, J. Biol. Chem. 267:25196–25201.PubMedGoogle Scholar
- Paulike, M., Nowack, D. D., and Morré, J. D., 1988, Isolation of a vesicular intermediate in the cell-free transfer of membrane from transitional elements of the endoplasmic reticulum to Golgi apparatus cisternae of rat liver, J. Biol. Chem. 263:17738–17748.Google Scholar