| First Author | Partridge EA | Year | 2004 |
| Journal | Science | Volume | 306 |
| Issue | 5693 | Pages | 120-4 |
| PubMed ID | 15459394 | Mgi Jnum | J:93100 |
| Mgi Id | MGI:3055715 | Doi | 10.1126/science.1102109 |
| Citation | Partridge EA, et al. (2004) Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis. Science 306(5693):120-4 |
| abstractText | 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. |
