Regulation of Cytokine Receptors by Golgi N-Glycan Processing and Endocytosis

@article{Partridge2004RegulationOC,
  title={Regulation of Cytokine Receptors by Golgi N-Glycan Processing and Endocytosis},
  author={Emily A. Partridge and Christine Le Roy and Gianni M. Di Guglielmo and Judy Pawling and Pam Cheung and Maria Granovsky and Ivan Robert Nabi and Jeffrey L. Wrana and James W. Dennis},
  journal={Science},
  year={2004},
  volume={306},
  pages={120 - 124}
}
The Golgi enzyme β1,6 N-acetylglucosaminyltransferase V (Mgat5) is up-regulated in carcinomas and promotes the substitution of N-glycan with poly N-acetyllactosamine, the preferred ligand for galectin-3 (Gal-3). Here, we report that expression of Mgat5 sensitized mouse cells to multiple cytokines. Gal-3 cross-linked Mgat5-modified N-glycans on epidermal growth factor and transforming growth factor–β receptors at the cell surface and delayed their removal by constitutive endocytosis. Mgat5… 
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657 Citations

Complex N-glycan and metabolic control in tumor cells.

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A systems approach to cancer treatment where the surface distribution of receptors is targeted through metabolism and N-glycan branching to induce growth arrest is suggested.

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Metabolic homeostasis and tissue renewal are dependent on beta1,6GlcNAc-branched N-glycans.

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Galectin Binding to Mgat5-Modified N-Glycans Regulates Fibronectin Matrix Remodeling in Tumor Cells

The results demonstrate that fibronectin polymerization and tumor cell motility are regulated by galectin-3 binding to branched N-glycan ligands that stimulate focal adhesion remodeling, FAK and PI3K activation, local F-actin instability, and α5β1 translocation to fibrillar adhesions.

Cytokine sensitivity and N-glycan processing mutations.

Assembly, organization and regulation of cell-surface receptors by lectin-glycan complexes.

In the present review, the data available on the assembly, hierarchical organization and regulation of conspicuous galectin-glycan complexes, and their implications in health and disease are summarized.

Adaptive Regulation at the Cell Surface by N‐Glycosylation

Computational modelling of the hexosamine/Golgi/lattice has provided new insight on cell surface adaptation in cancer and autoimmune disease.

VIP36 preferentially binds to core-fucosylated N-glycans: a molecular docking study

This fundamental approach with large scale docking of 165 carbohydrates suggests, that linked cargo-receptor apical transport may provide a path to epithelial polarization that may be modulated by core fucosylation.
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