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Sci. Signal., 20 December 2011
Vol. 4, Issue 204, p. ra89
Developing with Intracellular O-Glycosylation
Modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a reversible posttranslational modification that occurs on cytoplasmic and nuclear proteins and, like phosphorylation, appears to serve a regulatory function. Deficiency in the enzymes that control protein O-GlcNAcylation or in the biosynthetic pathways, such as the hexosamine biosynthetic pathway, that produce the precursors required for this modification cause developmental defects. Mariappa et al. showed that fruit flies defective in the hexosamine biosynthetic pathway exhibited reduced protein O-GlcNAcylation and were specifically defective in activation of mitogen-activated protein kinase downstream of fibroblast growth factor (FGF), but not downstream of other receptor tyrosine kinases. They identified the FGF receptor–specific adaptor protein Dof as the target for O-GlcNAcylation. Thus, modification of the FGF receptor complex by O-GlcNAc appears to be critical for this key developmental pathway.
Citation: D. Mariappa, K. Sauert, K. Mariño, D. Turnock, R. Webster, D. M. F. van Aalten, M. A. J. Ferguson, H.- A. J. Müller, Protein O-GlcNAcylation Is Required for Fibroblast Growth Factor Signaling in Drosophila. Sci. Signal.4, ra89 (2011).