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. 2004 Oct 1;306(5693):120-4.
doi: 10.1126/science.1102109.

Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis

Emily A Partridge  1 , Christine Le Roy, Gianni M Di Guglielmo, Judy Pawling, Pam Cheung, Maria Granovsky, Ivan R Nabi, Jeffrey L Wrana, James W Dennis
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Free article

Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis

Emily A Partridge et al. Science. .
Free article

Abstract

The Golgi enzyme beta1,6 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-beta receptors at the cell surface and delayed their removal by constitutive endocytosis. Mgat5 expression in mammary carcinoma was rate limiting for cytokine signaling and consequently for epithelial-mesenchymal transition, cell motility, and tumor metastasis. Mgat5 also promoted cytokine-mediated leukocyte signaling, phagocytosis, and extravasation in vivo. Thus, conditional regulation of N-glycan processing drives synchronous modification of cytokine receptors, which balances their surface retention against loss via endocytosis.

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