title: Role of N- and O-glycans in polarized biosynthetic sorting.
abstract: The maintenance of proper epithelial function requires efficient sorting of newly synthesized and recycling proteins to the apical and basolateral surfaces of differentiated cells. Whereas basolateral protein sorting signals are generally confined to their cytoplasmic regions, apical targeting signals have been identified that localize to luminal, transmembrane, and cytoplasmic aspects of proteins. In the past few years, both N- and O-linked glycans have been identified as apical sorting determinants. Glycan structures are extraordinarily diverse and have tremendous information potential. Moreover, because the oligosaccharides added to a given protein can change depending on cell type and developmental stage, the potential exists for altering sorting pathways by modulation of the expression pattern of enzymes involved in glycan synthesis. In this review, we discuss the evidence for glycan-mediated apical sorting along the biosynthetic pathway and present possible mechanisms by which these common and heterogeneous posttranslational modifications might function as specific sorting signals.
authors.affiliation: Laboratory of Epithelial Cell Biology, Renal-Electrolyte Division, Univ. of Pittsburgh School of Medicine, 978 Scaife Hall, 3550 Terrace St., Pittsburgh, PA 15261, USA.
authors.forename: Beth A
authors.initials: BA
authors.lastname: Potter
authors.forename: Rebecca P
authors.initials: RP
authors.lastname: Hughey
authors.forename: Ora A
authors.initials: OA
authors.lastname: Weisz
mesh_terms: D000818:Animals; D016764:Cell Polarity / Q000502:physiology*; D004847:Epithelial Cells / Q000166:cytology / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D006801:Humans; D007413:Intestinal Mucosa / Q000166:cytology / Q000378:metabolism; D021381:Protein Transport / Q000502:physiology*
chemical_list: D006023:Glycoproteins