title: Carbohydrate-mediated Golgi to cell surface transport and apical targeting of membrane proteins.
abstract: Polarized expression of most epithelial plasma membrane proteins is achieved by selective transport from the Golgi apparatus or from endosomes to a specific cell surface domain. In Madin-Darby canine kidney (MDCK) cells, basolateral sorting generally depends on distinct cytoplasmic targeting determinants. Inactivation of these signals often resulted in apical expression, suggesting that apical transport of transmembrane proteins occurs either by default or is mediated by widely distributed characteristics of membrane glycoproteins. We tested the hypothesis of N-linked carbohydrates acting as apical targeting signals using three different membrane proteins. The first two are normally not glycosylated and the third one is a glycoprotein. In all three cases, N-linked carbohydrates were clearly able to mediate apical targeting and transport. Cell surface transport of proteins containing cytoplasmic basolateral targeting determinants was not significantly affected by N-linked sugars. In the absence of glycosylation and a basolateral sorting signal, the reporter proteins accumulated in the Golgi complex of MDCK as well as CHO cells, indicating that efficient transport from the Golgi apparatus to the cell surface is signal-mediated in polarized and non-polarized cells.
authors.affiliation: Department of Cell Biology, University of Geneva, Geneva, Switzerland.
authors.forename: A
authors.initials: A
authors.lastname: Gut
authors.forename: F
authors.initials: F
authors.lastname: Kappeler
authors.forename: N
authors.initials: N
authors.lastname: Hyka
authors.forename: M S
authors.initials: MS
authors.lastname: Balda
authors.forename: H P
authors.initials: HP
authors.lastname: Hauri
authors.forename: K
authors.initials: K
authors.lastname: Matter
mesh_terms: D000818:Animals; D001692:Biological Transport; D016466:CHO Cells; D002460:Cell Line; D002462:Cell Membrane; D016764:Cell Polarity / Q000502:physiology*; D006224:Cricetinae; D004285:Dogs; D006031:Glycosylation / Q000187:drug effects; D006056:Golgi Apparatus / Q000378:metabolism*; D037241:Mannose-Binding Lectins; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D062793:Occludin; D009844:Oligosaccharides; D011961:Receptors, Fc / Q000235:genetics / Q000378:metabolism; D011973:Receptors, LDL / Q000235:genetics; D011993:Recombinant Fusion Proteins; D014415:Tunicamycin / Q000494:pharmacology
chemical_list: D037241:Mannose-Binding Lectins; D008565:Membrane Proteins; D062793:Occludin; D009844:Oligosaccharides; D011961:Receptors, Fc; D011973:Receptors, LDL; D011993:Recombinant Fusion Proteins; D014415:Tunicamycin