Abstract
Newly synthesized surface glycoproteins undergo extensive processing of their N-linked oligosaccharides during transport from the endoplasmic reticulum to the cell surface (for review Kornfeld and Kornfeld 1985). The fundamental processing reactions include removal of glucose and mannose residues from Glc3Man9GlcNAc2 by glucosidases I and II and several mannosidases in the endoplasmic reticulum and the cis-Golgi to generate Man5GlcNAc2 which is the preferred substrate for N-acetylglucosaminyltransferase I of the medial Golgi compartment generating GlcNAcMan5GlcNAc2. This structure can be acted upon by different enzymes including Nacetylglucosaminyltransferase III, N-acetylglucosaminyltransferase IV or can move from the medial to the trans-Golgi to form different types of hybrid structures. Alternatively, two additional mannose residues can be removed from GlcNAcMan5GlcNAc2 by α-mannosidase II in the medial Golgi to form GlcNAcMan3GlcNAc2, which can be acted upon by N-acetylglucosaminyltransferase II, III or IV, or by α6-fucosyltransferase, or can enter the trans-Golgi where the outer chains are extended by galactosyl-, fucosyl-, and sialyltransferases (Schachter 1986). Since the multiple processing enzymes may act upon the oligosaccharide substrates in various combinations, this nontemplate assembly line is perfectly suited to generate the wide variety of oligosaccharide structures found in secretory and membrane glycoproteins.
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© 1994 Springer-Verlag Berlin Heidelberg
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Tauber, R. et al. (1994). Reprocessing of Membrane Glycoproteins. 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_12
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DOI: https://doi.org/10.1007/978-3-642-78729-4_12
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