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Organization of the Glycoprotein and Polysaccharide Synthetic Pathways in the Plant Golgi Apparatus

  • L. A. Staehelin
Conference paper
Part of the NATO ASI Series book series (volume 74)

Abstract

The Golgi apparatus serves as a processing and sorting station for secretory proteins as they pass from their site of origin, the endoplasmic reticulum, to their final destination, the cell surface or the lysosomal/vacuolar systems. There is general consensus that in animal cells the Golgi apparatus consists of at least four distinct functional compartments known as cis, medial and trans Golgi cisternae, and the trans Golgi network (TGN) (Farquhar, 1985; Griffiths and Simons, 1986). Proteins enter the stack at its cis face and depart from the opposite trans face (Dunphy and Rothman, 1985), and transport between the cisternal compartments is mediated by transport vesicles (Duden et al., 1991). The definition of these compartments is based on biochemical fractionation studies, as well as on the histochemical and immuno-cytochemical localization of specific glycosyltransferases and their products (Kornfeld and Kornfeld, 1985; Roth, 1987). Cis Golgi cisternae contain the enzyme N-acetylglucosamine (GlcNAc)-1-phosphodiester α-N-acetylglucosaminidase, which is involved in the addition of mannose 6-phosphate residues to the oligosaccharide side chains of lysosomal enzymes. The enzyme GlcNAc transferase I is found in the medial cisternae, whereas most of the galactosyltransferase activity is located in the trans cisternae. The addition of terminal sialic acid residues, finally, is largely confined to the TGN. Thus the presence of a specific type of Golgi compartment in a biochemical fraction can be defined by the presence of specific marker enzyme activities, and the types of cisternae through which a given N-linked glycoprotein has passed can be determined by the types of modifications that are present on its oligosaccharide side chain(s). This knowledge of the functional organization of the Golgi apparatus has proven immensely valuable for designing experiments to explore mechanisms of trafficking through the Golgi apparatus of animal cells, and for deciphering the sites of action of drugs such as brefeldin A that interfere with the secretory pathway.

Keywords

Golgi Apparatus Trans Golgi Network Pectic Polysaccharide Golgi Cisterna Golgi Stack 
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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References

  1. Baron-Epel 0, Gharyal P, Schindler M (1988) Pectins as mediators of wall porosity in soybean cells. Planta 175: 389 - 395CrossRefGoogle Scholar
  2. Duden R, Allan V, Kreis T (1991) Involvement of ß-COP in membrane traffic through the Golgi complex. Trends Cell Biol. 1: 14 - 19PubMedCrossRefGoogle Scholar
  3. Dunphy WG, Rothman JE (1985) Compartmental organization of the Golgi stack. Cell 42: 13 - 21PubMedCrossRefGoogle Scholar
  4. Farquhar MG (1985) Progress in unraveling pathways of Golgi traffic. Ann Rev Cell Biol 1: 447 - 488PubMedCrossRefGoogle Scholar
  5. Faye L, Johnson KD, Stern, A, Chrispeels MJ (1989) Structure, biosynthesis, and function of asparagine-linked glycans of plant glycoproteins. Physiol Plant 75: 309 - 314CrossRefGoogle Scholar
  6. Fry SC, Smith RC, Renwick KF, Martin DJ, Hodge SK, Mathews KJ (1992) Xyloglucan endotransglycolase, a new wall-loosening enzyme activity from plants. Biochem J 282: 821 - 828PubMedGoogle Scholar
  7. Garcia-Herdugo G, Gonzales-Reyes JA, Garcia-Navarro F, Navas P (1988) Growth kinetics of the Golgi apparatus during the cell cycle in onion root meristems. Planta 175: 305 - 312CrossRefGoogle Scholar
  8. Griffiths G, Simons K (1986) The trans Golgi network: Sorting at the exit site of the Golgi complex. Science 234: 438-443Google Scholar
  9. Hayashi T (1989) Xyloglucans in the primary cell wall. Ann Rev Plant Physiol Mol Biol 40: 139 - 168CrossRefGoogle Scholar
  10. Jarvis MC (1984) Structure and properties of pectin gels in plant cell walls. Plant Cell and Envir 7: 153 - 164Google Scholar
  11. Kornfeld R, Kornfeld S (1985) Assembly of asparagine-linked oligosaccharides. Ann Rev Biochem 54: 631 - 664PubMedCrossRefGoogle Scholar
  12. Lynch MA, Staehelin LA (1992) Domain-specific and cell-type specific localization of two types of cell wall matrix polysaccharides in the clover root tip. J Cell Biol (in press)Google Scholar
  13. McNeil M, Darvill AG, Fry SC, Albersheim P (1984) Structure and function of the primary cell walls of plants. Ann Rev Biochem 8: 625 - 663CrossRefGoogle Scholar
  14. Moore PJ, Darvill A, Albersheim P, Staehelin, LA (1986) Immunogold localization of xyloglucan and rhamnogalacturonan I in the cell walls of suspension-cultured sycamore cells. Plant Physiol 82: 787 - 794PubMedCrossRefGoogle Scholar
  15. Rambourg A, Clermont Y (1990) Three dimensional microscopy: structure of the Golgi apparatus. Eur J Cell Biol 51: 189PubMedGoogle Scholar
  16. Roth J (1987) Subcellular organization of glycosylation in mammalian cells. Biochem Biophys Acta 906: 405 - 436PubMedCrossRefGoogle Scholar
  17. Ryan CA, Farmer EE (1991) Oligosaccharide signals in plants: a current assessment. Ann Rev Plant Physiol Mol Biol 42: 651 - 674CrossRefGoogle Scholar
  18. Staehelin LA, Giddings TH, Kiss JZ, Sack FD (1990) Macromolecular differentiation of Golgi stacks in root tips of Arabidopsis and Nicotiana seedlings as visualized in high pressure frozen and freeze-substituted samples. Protoplasma 157: 75 - 91PubMedCrossRefGoogle Scholar
  19. Sturm A, Johnson KD, Szumilo T, Elbein AD, Chrispeels MJ (1987) Subcellular localization of glycosidases and glycosyltransferases in the processing of N-linked oligosaccharides. Plant Physiol 85: 741 - 745PubMedCrossRefGoogle Scholar
  20. Vitale A, Chrispeels MJ (1992) Sorting of proteins to the vacuoles of plant cells. BioEssays 14: 151 - 160Google Scholar
  21. Zhang GF, Staehelin LA (1992) Functional compartmentalization of the Golgi apparatus of plant cells. An immunocytochemical analysis of high pressure frozen and freeze-substituted sycamore maple suspension culture cells. Plant Physiol 99 (in press)Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1993

Authors and Affiliations

  • L. A. Staehelin
    • 1
  1. 1.Department of Molecular and Cellular and Developmental BiologyUniversity of ColoradoBoulderUSA

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