Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 5 October 2004
Vol. 2004, Issue 253, p. tw358
[DOI: 10.1126/stke.2532004tw358]

EDITORS' CHOICE

RECEPTORS Sensitizing Cell-Surface Signaling

Signaling at the cell surface involves the interaction between cell-surface receptors and extracellular ligands and is often regulated by a process of receptor internalization that will tend to attenuate signaling in the continuing presence of ligand. Partridge et al. present evidence that the glycosylation state of certain receptors is a key factor in regulating their response to ligands because of its effects on the likelihood of receptor internalization. When a Golgi enzyme responsible for adding specific sugars to cell-surface receptors is upregulated in carcinomas, sensitivity to a variety of growth factors and cytokines is increased. It seems that the receptors become cross-linked together at the cell surface through the expression of the binding site for an endogenous lectin, Gal-3, and that this cell-surface web of receptors resists internalization, thereby prolonging responsiveness to growth factors.

E A. Partridge, C. Le Roy, G. M. Di Guglielmo, J. Pawling, P. Cheung, M. Granovsky, I. R. Nabi, J. L. Wrana, J. W. Dennis, Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis. Science 306, 120-124 (2004) [Abstract] [Full Text]

Citation: Sensitizing Cell-Surface Signaling. Sci. STKE 2004, tw358 (2004).


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882