Plant Golgi Apparatus

Abstract

The plant Golgi apparatus exists as a number of discrete units known as Golgi bodies distributed in the cytoplasm. Its primary roles are the glycosylation of secretory proteins, the construction of complex cell wall polysaccharides and the packaging and targeting of such products either to the vacuole or to the cell surface.

Keywords: plants; Golgi; cisternum; vesicles; secretion

Figure 1.

Microscopy of the plant Golgi apparatus. (a) The Golgi apparatus in living tobacco leaf epidermal cells. By expressing a chimaeric protein comprised of green fluorescent protein and a protein that recycles between the ER and Golgi (the HDEL receptor ERD2; see Boevink et al., ) the endomembrane system can be observed by confocal fluorescence microscopy. Golgi bodies (bright fluorescent dots arrowed) can be seen to be associated with the reticulate network of cortical ER tubules. Bar, 10 mm. (b) The Golgi apparatus can be located by immunofluorescence staining of glycan epitopes. In this onion prophase root tip cell observed by confocal microscopy, the Golgi bodies (small green fluorescent dots) are widely distributed throughout the cytoplasm. The antibody also stains the plasma membrane. Condensing chromatin (red) is stained with propidium iodide. Bar, 10 mm. (c) Transmission electron micrograph of two Golgi stacks in a maize root cap hypersecretory cell. Note the massive, slime‐producing vesicles associated with the medial‐ and trans‐Golgi. Bar, 300 nm. (d) Different views of Golgi in a pea root meristematic cell. The Golgi (G) and endoplasmic reticulum (ER) have been stained selectively by an osmium impregnation technique. In cross‐section, the stacks are more heavily stained at the cis‐face (small arrows). Fine tubules and vesicles are associated with the fenestrated margins of cisternae. This can be seen most clearly in stacks that have been sectioned in face view (large arrowheads). Bar, 500 nm.

Figure 2.

Pathway of N‐linked glycosylation events leading to the production of a complex bi‐antennary glycan. In the ER, the oligosaccharide precursor undergoes a glucosidase‐mediated trimming of the three terminal glucose residues (1). In the trans‐Golgi further trimming occurs when α‐mannosidase removes up to four mannose residues (2). Then a series of transferases sequentially add two terminal N‐acetyl glucosamine residues along with the removal of further mannose residues (3–4). Fucosyl and xylosyltransferases add fucose and xylose to N‐acetyl glucosamine and mannose residues on the core glycan, respectively (5). Finally, terminal fucose and/or galactose residues can be added to give the final complex glycan structure (6). Shown in the diagram is the formation of a complex glycan with terminal Lewis a antigens. Further processing of glycans can occur such as trimming by exoglycosidases en route to the vacuole (7).

Figure 3.

The maturation model for transport across the Golgi stack. Product and membrane are produced from domains in the ER and transported to the cis‐Golgi (via vesicles or tubules) where they coalesce to form a new cis‐cisterna. Within each cisterna secretory products (glycosylation of proteins and biosynthesis of wall material) are sequentially built through the action of transferases. At the medial‐ and trans‐side of the Golgi stack membrane is lost through conversion into secretory vesicles and clathrin‐coated vesicles. This membrane loss may also be partly balanced by an endocytic flow and retrograde shuttle of vesicles across the Golgi, where they help with the construction of new cis‐cisternae. (Claude Saint‐Jore is acknowledged for her help in constructing this diagram.)

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References

Becker B, Böllinger B and Melkonian M (1995) Anterograde transport of algal scales through the Golgi complex is not mediated by vesicles. Trends in Cell Biology 5: 305–307.

Boevink P, Oparka K and Santa Cruz S et al. (1998) Stacks on tracks: the plant Golgi apparatus traffics on an actin/ER network. Plant Journal 15: 441–447.

daSilva LL, Snapp EL and Denecke J et al. (2004) Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells. The Plant Cell 16: 1753–1771.

Hawes C (2004) Cell biology of the plant Golgi apparatus. New Phytologist 165: 29–44.

Hawes C and Satiat‐Jeunemaitre B (2005) The plant Golgi apparatus – going with the flow. Biochemica et Biophysica Acta 1744: 93–107.

Hawes C, Faye L and Satiat‐Jeunemaitre B (1996) The Golgi apparatus and pathways of vesicle trafficking. In: Smallwood M, Knox JP and Bowles DJ (eds) Membranes: Specialized Functions in Plants, pp. 337–365. Oxford: Bios

Knox JP (1996) Arabinogalactan‐proteins: developmentally regulated proteoglycans of the plant cell surface. In: Smallwood M, Knox JP and Bowles DJ (eds) Membranes: Specialized Functions in Plants, pp. 93–102. Oxford: Bios

Latijnhouwers M, Hawes C and Carvalho C (2005) Holding it all together? Candidate proteins for the plant Golgi matrix. Current Opinion in Plant Science 8: 1–8.

Munro S (1998) Localization of proteins to the Golgi apparatus. Trends in Cell Biology 8: 11–15.

Pagny S, Bouissonnie F and Sarkar M et al. (2003) Structural requirements for Arabidopsis beta1,2‐xylosyltransferase activity and targeting to the Golgi. Plant Journal 33: 189–203.

Rayon C, Lerouge P and Faye L (1998) The protein N‐glycosylation in plants. Journal of Experimental Botany 49: 1463–1472.

Robinson DG, Hinz G and Holstein SHE (1998) The molecular characterization of transport vesicles. Plant Molecular Biology 38: 49–76.

Satiat‐Jeunemaitre B, Steele C and Hawes C (1996) Golgi‐membrane dynamics are cytoskeleton dependent: a study of Golgi stack movement induced by brefeldin A. Protoplasma 191: 21–33.

Wee EG‐T, Sherrier JD, Prime TA and Dupree P (1998) Targeting of active sialyl transferase to the plant Golgi apparatus. Plant Cell 10: 1759–1768.

Wenzel D, Schauermann G, von Lüpke A and Hinz G (2005) The cargo in vacuolar storage protein transport vesicles is stratified. Traffic 6: 45–55.

Further Reading

doi/10.1199/tab.0009, http://www.aspb.org/publications/arabidopsis/.

Driouich A and Staehelin LA (1997) The plant Golgi apparatus: structural organization and functional properties. In: Berger EG and Roth J (eds) The Golgi Apparatus, pp. 275–300. Basel: Birkhäser‐Verlag

Duden R, Presley J and Storrie B (eds) (2005) The Golgi complex. Biochimica et Biophysica Acta, Molecular Cell Research 1744: 257–517.

Hanton SL, Bortolotti LE, Renna L, Stefano G and Brandizzi F (2005) Crossing the divide – transport between the endoplasmic reticulum and Golgi apparatus in plants. Traffic 6: 267–277.

Hawes CR, Coleman JOD and Evans DE (1991) Endocytosis, Exocytosis and Vesicle Traffic in Plants. Cambridge: Cambridge University Press.

Képès F, Rambourg A and Satiat‐Jeunemaitre B (2005) Morphodynamics of the secretory pathway. International Review of Cytology 242: 55–120.

Robinson DG (ed.) (2003) The Golgi Apparatus and the Plant Secretory Pathway. Annual Plant Reviews, vol. 9. Oxford: Blackwell Publishing.

Sanderfoot AA and Raikhel NV (2003) The secretory system of arabidopsis. In: Somerville CR and Meyerowitz EM (eds) The Arabidopsis Book. Rockville, MD: American Society of Plant Biologists.

Sherrier DJ and Vanden Bosch KA (1994) Secretion of cell wall polysaccharides in Vicia root hairs. Plant Journal 5: 185–195.

Staehelin LA and Moore I (1995) The plant Golgi apparatus. Annual Review of Plant Physiology and Plant Molecular Biology 46: 261–288.

Staehelin LA, Giddings TH Jr, Kiss JZ and 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: 75–91.

Various Authors (1998) Golgi centenary issue. Trends in Cell Biology 8: 1–49.

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How to Cite close
Hawes, Chris, and Satiat‐Jeunemaitre, Béatrice(Sep 2006) Plant Golgi Apparatus. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0001674.pub2]