O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts

@article{Alfalah1999OlinkedGM,
  title={O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts},
  author={Marwan Alfalah and Ralf Jacob and Ute Preuss and Klaus Peter Zimmer and Hussein Y. Naim and Hassan Y. Naim},
  journal={Current Biology},
  year={1999},
  volume={9},
  pages={593-S2}
}
The plasma membrane of polarised epithelial cells is characterised by two structurally and functionally different domains, the apical and basolateral domains. These domains contain distinct protein and lipid constituents that are sorted by specific signals to the correct surface domain [1]. The best characterised apical sorting signal is that of glycophosphatidylinositol (GPI) membrane anchors [2], although N-linked glycans on some secreted proteins [3] and O-linked glycans [4] also function as… Expand
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TLDR
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TLDR
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TLDR
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TLDR
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N-linked glycans containing linear poly-N-acetyllactosamine as sorting signals in endocytosis in Trypanosoma brucei
TLDR
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It is demonstrated that carbohydrates act as an apical targeting signal for secretory proteins, and glycans not only play a general role in protein folding but also appear to function in protein sorting in biosynthetic traffic. Expand
The O-glycosylated Stalk Domain Is Required for Apical Sorting of Neurotrophin Receptors in Polarized MDCK Cells
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The stalk domain is shown to be required for apical secretion of a soluble form of p75NTR, providing the first demonstration that the same domain can mediate apical sorting of both a membrane-anchored as well as secreted protein. Expand
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Results show that basolateral sorting signals are not always dominant over apical sorting signals in proteins that contain each and suggest that sorting of Basolateral from apical proteins occurs within a common compartment where competition for sorting signals can occur. Expand
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A high degree of homology between the isomaltase and sucrase portions (41% amino acid identity), indicating that pro-SI evolved by partial gene duplication. Expand
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The results demonstrate that an endogenous apical integral membrane glycoprotein of Madin-Darby canine kidney cells is sorted intracellularly and is vectorially targeted to the apical surface. Expand
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