A sweet spot in the FGFR signal transduction pathway.

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.

journal_name

Sci Signal

journal_title

Science signaling

authors

Ghabrial AS

doi

10.1126/scisignal.2002789

subject

Has Abstract

pub_date

2012-01-17 00:00:00

pages

pe1

issue

207

eissn

1945-0877

issn

1937-9145

pii

scisignal.2002789

journal_volume

5

pub_type

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