Abstract
The entire output of proteins newly synthesized in the endoplasmic reticulum (ER) is funneled through the Golgi stack and sorted once it reaches the trans Golgi network (TGN) (Griffiths and Simons 1986). Up until this point, transport occurs by default, no signals being needed for proteins to move from the ER to the Golgi and from cis-terna to cisterna within the stack (Rothman and Orci 1992). This immediately raises the question of how proteins are retained along the secretory pathway; how do they resist transport to the TGN if such transport has no need of specific signals?
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References
Aoki D, Lee N, Yamaguchi N, Dubois C, Fukuda MN (1992) Golgi retention of a trans-Golgi membrane protein, galactosyltransferase, requires cysteine and histidine residues within the membrane-anchoring domain. Proc Natl Acad Sci USA 89:4319–23
Baron MD, Garoff H (1990) Mannosidase II and the 125-kDa Golgi-specific antigen recognised by monoclonal antibody 53FC3 are the same dimeric protein. J Biol Chem 265:19928–19931
Burke B, Warren G (1984) Microinjection of mRNA coding for anti-Golgi antibody inhibits intracellular transport of a viral membrane protein. Cell 36:847–856
Burke J, Pettitt JM, Schachter H, Sarkar M, Gleeson PA (1992) The transmembrane and flanking sequences of β1,2-N-acetylglucosaminyltransferase I specify medial-Golgi localization. J Biol Chem 267:24433–24440
Colley KJ, Lee EU, Paulson JC (1992) The signal anchor and stem regions of the b-galactoside α2,6-sialyltransferase may each act to localize the enzyme to the Golgi apparatus. J Biol Chem 267:7784–7793
Fleischer B, Mclntyre JO, Kempner ES (1993) Target size of galactosyltransferase, sialyltrans- ferase and uridine diphosphatase in Golgi apparatus of rat liver. Biochemistry 32:2076–2081
Griffiths G, Simons K (1986) The trans Golgi network: sorting at the exit site of the Golgi complex. Science 234:438–443
Jackson MR, Nilsson T, Peterson PA (1993) Retrieval of transmembrane proteins to the endoplasmic reticulum. J Cell Biol 121:317–333
Khatra BS, Herries DG, Brew K (1974) Some kinetic properties of human-milk galactosyl- transferase. Eur J Biochem 44:537–560
Lucocq JM, Berger EG, Warren G (1989) Mitotic Golgi fragments in HeLa cells and their role in the reassembly pathway. J Cell Biol 109:463–474
Malhotra V, Serafini T, Orci L, Shepherd JC, Rothman JE (1989) Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack. Cell 58:329–336
Marks MS, Blum JS, Cresswell P (1990) Invariant chain trimers are sequestered in the rough endoplasmic reticulum in the absence of association with HLA class II antigens. J Cell Biol 111:839–855
Moremen KW, Touster O, Robbins PW (1991) Novel purification of the catalytic domain of Golgi α-mannosidase II. Characterization and comparison with the intact enzyme. J Biol Chem 266:16876–16885
Munro S (1991) Sequences within and adjacent to the transmembrane segment of α-2,6-sialyl- stransferase specify Golgi retention. EMBO J 10:3577–3588
Navaratnam N, Ward S, Fisher C, Kuhn NJ, Keen JN, Findlay JBC (1988) Purification, properties and cation activation of galactosyltransferases from lactating-rat mammary Golgi membranes. Eur J Biochem 171:623–629
Nilsson T, Lucocq JM, Mackay D, Warren G (1991) The membrane spanning domain of β-1,4- galactosyltransferase specifies trans Golgi retention. EMBO J 10:3567–3575
Nilsson T, How MH, Slusarewicz P, Rabouille C, Watson R, Hunte F, Watzele G, Berger EG, Warren G (1994) Kin recognition between medial Golgi enzymes in HeLa cells. EMBO J (in press)
Pearse BMF (1987) Clathrin and coated vesicles. EMBO J 6:2507–2512
Pelham HR (1989) Control of protein exit from the endoplasmic reticulum. Ann Rev Cell Biol 5:1–23
Rothman JE, Orci L (1992) Molecular dissection of the secretory pathway. Nature 355:409–416
Russo RN, Shaper NL, Taatjes DJ, Shaper JH (1992) βl,4-galactosyltransferase: a short NH2- terminal fragment that includes the cytoplasmic and transmembrane domain is sufficient for Golgi retention. J Biol Chem 267:9241–9247
Slusarewicz P, Nilsson T, Hui N, Watson R, Warren G (1994) Isolation of a intercisternal matrix that binds medial Golgi enzymes. J Cell Biol (in press)
Smith S, Blobel G (1993) The first membrane spanning region of the lamin B receptor is sufficient for sorting to the inner nuclear membrane. J Cell Biol 120:631–637
Sweet DJ, Pelham HRB (1992) The S. cerevisiae SEC20 gene encodes a membrane glycoprotein which is sorted by the -HDEL retrieval system. EMBO J 11:423–432
Swift AM, Machamer CE (1991) A Golgi retention signal in a membrane-spanning domain of coronavirus-El protein. J Cell Biol 115:19–30
Tang BL, Wong SH, Low SH, Hong W (1992) The transmembrane domain of N-glucosami- nyltransferase I contains a Golgi retention signal. J Biol Chem 267:10122–10126
Teasdale RD, D’Agostaro G, Gleeson PA (1992) The signal for Golgi retention of bovine β1,4- galactosyltransferase is in the transmembrane domain. J Biol Chem 267:4084–4096
Wong SH, Low SH, Hong W (1992) The 17-residue transmembrane domain of the β-galacto- side α2,6-sialyltransferase is sufficient for Golgi retention. J Cell Biol 117:245–258
Wozniak RW, Blobel G (1992) The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope. J Cell Biol 119:1441–1449
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© 1994 Springer-Verlag Berlin Heidelberg
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Nilsson, T., Souter, E., Watson, R., Warren, G. (1994). Protein Retention in the Golgi Stack. In: Wieland, F., Reutter, W. (eds) Glyco-and Cellbiology. Colloquium der Gesellschaft für Biologische Chemie 22.–24. April 1993 in Mosbach/Baden, vol 44. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78729-4_3
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DOI: https://doi.org/10.1007/978-3-642-78729-4_3
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