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.

Subscribe

Sci. Signal., 17 January 2012
Vol. 5, Issue 207, p. pe1
[DOI: 10.1126/scisignal.2002789]

PERSPECTIVES

A Sweet Spot in the FGFR Signal Transduction Pathway

Amin S. Ghabrial*

Department of Cell and Developmental Biology, Perelman School of Medicine, University of Pennsylvania, PA 19104, USA.

Abstract: The hexosamine biosynthetic pathway, whose end product is UDP-N acetylglucosamine (UDP-GlcNAc), lies at the base of cellular glycosylation pathways, including glycosylation of lipids, formation of heparin sulfated proteoglycans, and N- and O-linked glycosylation of proteins. Forward genetic studies in Drosophila have revealed that mutations in genes encoding different enzymes of the hexosamine biosynthetic pathway result in reduction of UDP-GlcNAc to different extents, with a consequent disruption of distinct glycosylation pathways and developmental processes. A maternal and zygotic loss-of-function screen has identified mutations in nesthocker (nst), which encodes an enzyme in the hexosamine biosynthetic pathway. Embryos lacking maternal and zygotic nst gene products show defective O-GlcNAcylation of a fibroblast growth factor receptor (FGFR)–specific adaptor protein, which impairs FGFR-dependent migration of mesodermal and tracheal cells.

* Corresponding author. E-mail, ghabrial{at}mail.med.upenn.edu

Citation: A. S. Ghabrial, A Sweet Spot in the FGFR Signal Transduction Pathway. Sci. Signal. 5, pe1 (2012).

Read the Full Text



To Advertise     Find Products


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