Abstract
In this chapter, we summarize important findings in the field of intracellular transport, which have considerably contributed to the understanding of the function and organization of the Golgi apparatus (GA). It is not possible to mention all authors in this huge field. We apologize for gaps and incompleteness, and are thankful for suggestions and corrections.
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References
Bainton DF, Faruhar MG (1966) Origin of granules in polymorphonuclearleuk ocytes. Two types derived from opposite faces of the Golgi complex in developing granulocytes. J Cell Biol 28(2): 277–301
Balch WE, Dunphy WG, Braell WA, Rothman JE (1984) Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine. Cell 39: 405–416
Bannykh SI, Rowe T, Balch WE (1996) The organization of endoplasmicreticulum export complexes. J Cell Biol 135: 19–35
Bannykh SI, Balch WE (1997) Membrane dynamics at the endoplasmic reticulum-Golgi interface. J Cell Biol 138: 1–4
Barlowe C, Orci L, Yeung T, Hosobuchi M, Hamamoto S, Salama N, Rexach MF, Ravazzola M, Amherdt M, Schekman R (1994) COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77:895–907
Becker B, Bolinger B, Melkonian M (1995) Antero grade transport of algal sca les through the Golgi complex is not mediated by vesicles. Trends Cell Biol 5: 305–307
Berger EG (1997) The Golgi apparatus: from discovery to contemporary studies. In: Berger EG, Roth J (eds) The Golgi apparatus. Basel et al., Birkhauser Verlag, pp 1–35
Bonfanti L, Mironov AA Jr, Martinez-Menà rguez JA, Martella O, Fusella A, Baldassarre M, Buccione R, Geuze HJ, Mironov AA, Luini A (1998) Procollagen traverses the Golgi stack without leaving the lumen of cisternae: evidence for cisternal maturation. Cell 95(7): 993–1003
Cole NB, Smith CL, Sciaky N, Terasaki M, Edidin M, Lippincott-Schwartz J (1996) Diffusional mobility of Golgi proteins in membranes of living cells. Science 273(5276): 797–801
Cosson P, Letourneur F (1994) Coatomer interaction with di-lysine endoplasmic reticulum retention motif. Science 263: 1629–1631
Dalton AJ (1951) Observations of the Golgi substance with the electron microscope. Nature 168(4267): 244–245
De Matteis MA, Santini G, Kahn RA, Di Tullio G, Luini A (1993) Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex. Nature 364: 818–821
Dell’Angelica EC, Ohno H, Ooi CE, Rabinovich E, Roche KW, Bonifacino JS (1997) AP-3: an adaptor-like protein complex with ubiquitous expression. EMBO J 16(5): 917–928
Dell’Angelica EC, Mullins C, Bonifacino JS (1999) AP-4, a novel protein complex related to clathrin adaptors. J Biol Chem 274: 7278–7285
Doms RW, Russ G, Yewdell JW (1989) Brefeldin A redistributes resident and itinerant Golgi proteins to the end oplasmic reticulum. J Cell Biol 109: 61–72
Droscher A (1998) Camillo Golgi and the discovery of the Golgi apparatus. Histochem Cell Biol 109:425–430
Dunphy WG, Rothman JE (1983) Compartmentation of asparagine-linked oligosaccharide processing in the Golgi apparatus. J Cell Biol 97(1): 270–275
Farquhar MG, Palade GE (1981) The Golgi apparatus (complex)-(1954–1981)-from artifact to center stage. J Cell Biol 91(3 Pt 2): 77S–103S
Fasshauer D, Sutton RB, Brunger AT, John R (1998) Conserved structura l features of the synapticfusion complex: SNARE proteins reclassified as Q-and R-SNAREs. Proc Natl Acad Sci USA 95(26): 15781–15786
Featherstone C, Griffiths G, Warren G (1985) Newly synthesized G protein of vesicular stomatitis virus is not transported to the Golgi complex in mitotic cells. J Cell Biol 101(6): 2036–2046
Franke WW, Morre DJ, Deumling B, Cheetham RD, Kartenbeck J, Jarasch E-D, Zengtraf HW (1971) Synthesis and turnover of membrane proteins in rat liver: an examination of the membrane flow hypothesis. Z Naturforsch 26b: 1031–1039
Friend DS, Farquhar MG (1967) Functions of coated vesicles during protein absorption in the rat vas deferens. J Cell Biol 35(2): 357–376
Glick BS, Elston T, Oster G (1997) A cisternal maturation mechanism can explain the asymmetry of the Golgi stack. FEBS Lett 414: 177–181
Godman GC, Lane N (1964) On the site of sulfation in the chondrocyte. J Cell Biol 21: 353–366
Golgi C (1898a) Intorno alla struttura della cellula nervosa. Boll Soc Med Chir Pavia 13: 1–14
Golgi C (1898b) Surla structure des cellules nerveuses des ganglions spinaux. Arch Ital Biol 30: 60–71
Grasse PP (1957) Ultrastructure, polarity and reproduction of Golgi apparatus. C R Hebd Seances Acad Sci 245(16): 1278–1281
Griffiths G, Warren G, Stuhlfauth I, Jockusch BM (1981) The role of clathrin-coated vesicles in acrosome formation. Eur J Cell Biol 26(1): 52–60
Griffiths G, Simons K (1986) The trans Golgi network: sorting at the exit site of the Golgi complex. Science 34: 438–443
Happe S, Weidman P (1998) Cell-free transport to distinct Golgi cisternae is compartment specific and ARF independent. J Cell Biol 140(3): 511–523
Herzog V, Farquhar MG (1977) Luminal membrane retrieved after exocytosis reaches most Golgi cisternae in secretory cells. Proc Natl Acad Sci USA 74(11): 5073–5077
Hirschberg K, Miller CM, Ellenberg J, Presley JF, Siggia ED, Phair RB, Lippincott-Schwartz J (1998) Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport in living cells. J Cell Biol 143: 1485–1503
Jamieson JD, Palade GE (1967a) Intracellular transport of secretory proteins in the pancreatic exocrine cell. I. Role of the peripheral elements of the Golgi complex. J Cell Biol 34(2): 577–596
Jamieson JD, Palade GE (1967b) Intracellular transport of secretory proteins in the pancreatic exocrine cell. II. Transport to condensing vacuoles and zymogen granules. J Cell Biol 34(2): 597–615
Jamieson JD, Palade GE (1968a) Intracellular transport of secretory proteins in the pancreatic exocrine cell. 3. Dissociation of intracellular transport from protein synthesis. J Cell Biol 39(3): 580–588
Jamieson JD, Palade GE (1968b) Intracellular transport of secretory proteins in the pancreatic exocrine cell. IV. Metabolic requirements. J Cell Biol 39(3): 589–603
Jekely G (2003) Small GTPases and the evolution of the eukaryotic cell. Bioessays 25(11): 1129–1138
Kaiser CA, Schekman R (1990) Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway. Cell 61(4): 723–733
Kreitzer G, Schmoranzer J, Low SH, Li X, Gan Y, Weimbs T, Simon SM, Rodriguez-Boulan E (2003) Three-dimensional analysis of post-Golgi carrier exocytosis in epithelial cells. Nat Cell Biol 5(2): 126–136
Ladinsky MS, Mastronarde DN, McIntosh JR, Howell KE, Staehelin LA (1999) Golgi structure in three dimensions: functional insights from the normal rat kidney cell. J Cell Biol 144: 1135–1149
Lippincott-Schwartz J, Yuan LC, Bonifacino JS, Klausner RD (1989) Rapid redistribution of Golgi proteins into the ER in cells treated with Brefeldin A: evidence for membrane cycling from the Golgi to ER. Cell 56: 801–813
Lucocq JM, Pryde JG, Berger EG, Warren G (1987) A mitotic form of the Golgi apparatus in Hela cells. J Cell Biol 104: 865–874
Marra P, Salvatore L, Mironov A Jr, Di Campli A, Di Tullio G, Trucco A, Beznoussenko G, Mironov A, De Matteis MA (2007) The biogenesis of the Golgi ribbon: the roles of membrane input from the ER and of GM130. Mol Biol Cell 18(5): 1595–1608
Marsh BJ, Volkmann N, McIntosh JR, Howell KE (2004) Direct continuities between cisternae at different levels of the Golgi complex in glucose-stimulated mouse islet beta cells. Proc Natl Acad Sci USA 101(15): 5565–5570
Mironov AA, Weidman P, Luini A (1997) Variations on the intracellular transport theme: maturing cisternae and trafficking tubules. J Cell Biol 138: 481–484
Mironov AA, Beznoussenko GV, Nicoziani P, Martella O, Trucco A, Kweon HS, Di Giandomenico D, Polishchuk RS, Fusella A, Lupetti P, Berger EG, Geerts WJ, Koster AJ, Burger KN, Luini A (2001) Small cargo proteinsand large aggregates can traverse the Golgi by a common mechanism without leaving the lumen of cisternae. J Cell Biol 155: 1225–1238
Mironov AA, Mironov AA Jr, Beznoussenko GV, Trucco A Lupetti P, Smith JD, Geerts WJ, Koster AJ, Burger KN, Martone ME, Deerinck TJ, Ellisman MH, Luini A (2003) ER-to-Golgi carriers arise through direct en bloc protrusion and multistage maturation of specialized ER exit domains. Dev Cell 5: 583–594
Mironov AA, Beznoussenko GV, Polishchuk RS, Trucco A (2005) Intra-Golgi transport. A way to a new paradigm? BBA Mol Cell Res 1744: 340–350
Morre DJ, Mollenhauer HH (1964) Isolation of Golgi apparatus from plant cells. J Cell Biol 23: 295–305
Morre DJ, Merlin L, Keenan T (1969) Localization of glycosyl transferase activities in a Golgi apparatus-rich fraction isolated from rat liver. Biochem Biophys Res Commun 37(5): 813–819
Moya M, Dautry-Varsat A, Goud B, Louvard D, Boquet P (1985) Inhibition of coated pit formation in Hep2 cells blocks the cytotoxicity of diphtheria toxin but not that of ricin. J Cell Biol 101: 548–559
Munro S, Pelham HRB (1987) A C-terminal signal prevents secretion of luminal ER proteins. Cell 48: 899–907
Nakamura N, Rabouille C, Watson R, Nilsson T, Hui N, Slusarewicz P, Kreis TS, Warren G (1995) Characterization of a cis-Golgi matrix protein, GM130. J Cell Biol 131: 1715–1726
Neutra M, Leblond CP (1966) Radioautographic comparison of the uptake of galactose-H and glucose-H3 in the Golgi region of various cells secreting glycoproteins or mucopolysaccharides. J Cell Biol 30: 137–150
Newman AP, Shim J, Ferro-Novick S (1990) BET1, BOS1, and SEC22 are members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complex. Mol Cell Biol 10(7): 3405–3414
Novikoff A, Goldfischer S (1961) Nucleosidediphosphatase activity in the Golgi apparatus and its usefulness for cytological studies. Proc Natl Acad Sci USA 47: 802–810
Novikoff AB (1964) GERL, its form and function in neurons of rat spinal ganglia. Biol Bull 127:358
Novikoff AV, Essner E, Quintana N (1964) Golgi apparatus and lysosomes. Fed Proc 23: 1010–1022
Oprins A, Rabouille C, Posthuma G, Klumperman J, Geuze HJ, Slot JW (2001) The ER to Golgi interface is the major concentration site of secretory proteins in the exocrine pancreatic cell. Traffic 2: 831–838
Orci L, Glick BS, Rothman JE (1986) A new type of coated vesicular carrier that appears not to contain clathrin: its possible role in protein transport within the Golgi stack. Cell 46: 171–184
Orci L, Perrelet A, Rothman JE (1998) Vesicles on strings: morphological evidence for processive transport within the Golgi stack. Proc Natl Acad Sci USA 95(5): 2279–2283
Ostermann J, Orci L, Tani K, Amherdt M, Ravazzola M, Elazar Z, Rothman JE (1993) Step wise assembly of functionally active transport vesicles. Cell 75(5): 1015–1025
Ostermann J (2001) Stoichiometry and kinetics of transport vesicle fusion with Golgi membranes. EMBO Rep 2(4): 324–329
Pavelka M, Ellinger A, Debbage P, Loewe C, Vetterlein M, Roth J (1998) Endocytic routes to the Golgi apparatus. Histochem Cell Biol 109: 555–570
Pearse BM (1976) Clathrin: a unique protein associated with intracellular transfer of membrane by coated vesicles. Proc Natl Acad Sci USA 73(4): 1255–1259
Perasso L, Grunow A, Bruntrup IM, B€olinger B, Melkonian M, Becker B (2000) The Golgi apparatus of the scaly green flagellate Scherffelia dubia: uncoupling of glycoprotein and polysaccharide synthesis during flagellar regeneration. Planta 210(4): 551–562
Polishchuk RS, Polishchuk EV, Marra P, Alberti S, Buccione R, Luini A, Mironov AA (2000) Correlative light-electron microscopy reveals the tubular-saccular ultrastructure of carriers operating between Golgi apparatus and plasma membrane. J Cell Biol 148(1): 45–58
Polishchuk RS, San Pietro E, Di Pentima A, Tete S, Bonifacino JS (2006) Ultrastructure of long-range transport carriers moving from the trans Golgi network to peripheral endosomes. Traffic 7: 1092–1103
Presley JF, Cole NB, Schroer TA, Hirschberg K, Zaal KJ, Lippincott-Schwartz J (1997) ER-to-Golgi transport visualized in living cells. Nature 389: 81–85
Puthenveedu MA, Bachert C, Puri S, Lanni F, Linstedt AD (2006) GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution. Nat Cell Biol 8: 238–248
Roth J, Berger EG (1982) Immunocytochemical localization of galactosyltransferase in HeLa cells: codistribution with thiamine pyrophosphatase in trans-Golgi cisternae. J Cell Biol 93(1): 223–229
Roth J, Berger EG (eds) (1997) The Golgi apparatus. Basel. Birkhauser
Rothman JE, Bursztyn-Pettegrew H, Fine RE (1980) Transport of the membrane glycoprotein of vesicular stomatitis virus to the cell surface in two stages by clathrincoated vesicles. J Cell Biol 86(1): 162–171
Rothman JE, Miller RL, Urbani U (1984) Intercompartmental transport in the Golgi complex is a dissociative process: facile transfer of membrane protein between two Golgi populations. J Cell Biol 99: 260–271
Sandvig K, Sundan A, Olsnes S (1985) Effect of potassium depletion of cells on their sensitivity to diphtheria toxin and pseudomonas toxin. J Cell Physiol 124: 54–56
Saraste J, Kuismanen E (1984) Pre-and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface. Cell 38(2): 535–549
Scales SJ, Pepperkok R, Kreis TE (1997) Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell 90: 1137–1148
Schekman R, Mellman I (1997) Does COPI go both ways? Cell 90: 197–200
Seraf ini T, Orci L, Amherdt M, Brunner M, Kahn RA, Rothman JE (1991 ) ADP ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell 67(2): 239–253
Slusarewicz P, Nilsson T, Hui N, Watson R, Warren G (1994) Isolation of a matrix that binds medial Golgi enzymes. J Cell Biol 124(4): 405–413
Swift AM, Machamer CE (1991) A Golgi retention signal in a membrane-spanning domain of coronavirus E1 protein. J Cell Biol 115(1): 19–30
Tabas I, Kornfeld S (1980) Biosynthetic intermediates of beta-glucuronidase contain high mannose oligosaccharides with blocked phosphate residues. J Biol Chem 255(14): 6633–6639
Trucco A, Polishchuk RS, Martella O, Di Pentima A, Fusella A, Di Giandomenico D, San Pietro E, Beznoussenko GV, Polishchuk EV, Baldassarre M, Buccione R, Geerts WJ, Koster AJ, Burger KN, Mironov AA, Luini A (2004) Secretory traffic triggers the formation of tubular continuities across Golgi sub-compartments. Nat Cell Biol 6(11): 1071–1081
Varki A, Cummings R, Esko J, Freeze H, Hart G, Marth J (1999) Essentials of glycobiology. Cold Spring Harbor Laboratory Press, Cold Spring Harbor
Wacker I, Kaether C, Kromer A, Migala A, Almers W, Gerdes HH (1997) Microtubule-dependent transport of secretory vesicles visualized in realtime witha GFP-tagged secretory protein. J Cell Sci 110: 1453–1463
Weisz OA, Swift AM, Machamer CE (1993) Oligomerization of a membrane protein correlates with its retention in the Golgi complex. J Cell Biol 122(6): 1185–1196
Whur P, Herscovics A, Leblond CP (1969) Radioautographic visualization of the incorporation of galactose-3H and mannose-3H by rat thyroids in vitro in relation to the stages of thyroglobulin synthesis. J Cell Biol 43: 289–311
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Mironov, A.A., Pavelka, M. (2008). The Golgi apparatus and main discoveries in the field of intracellular transport. In: Mironov, A.A., Pavelka, M. (eds) The Golgi Apparatus. Springer, Vienna. https://doi.org/10.1007/978-3-211-76310-0_2
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DOI: https://doi.org/10.1007/978-3-211-76310-0_2
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