Baeg G.H. and Perrimon N. (2000) Functional binding of secreted molecules to heparan sulfate proteoglycans in Drosophila. Curr. Opin. Cell Biol. 12: 575-580
Capdevila J. and Izpisua Belmonte J.C. (1999) Extracellular modulation of the hedgehog, Wnt, and TGF-ß signalling pathways during embryonic development. Curr. Opin. Genet. Devel. 9: 427-433
Burke R., Nellen D., Bellotto M., Hafen E., Senti K.A., Dickson B.J. and Basler K. (1999) Dispatched, a novel sterol-sensing domain protein dedicated to the release of cholesterol-modified hedgehog from signaling cells. Cell 99: 803-815
Members of the Hedgehog (Hh) family of secreted signaling proteins are limited in their range of action by a C-terminal cholesterol tether. In a genetic screen for mutants affecting Hedgehog signaling, the authors of this study identified a novel segment-polarity gene in Drosophila, dispatched (disp). The phenotypes caused by loss of hh and disp function are very similar. In the absence of Disp, cholesterol-modified but not cholesterol-free Hh is retained in Hh-producing cells, indicating that Disp functions to release cholesterol-anchored Hh. Disp and the putative Hh receptor, Patched, share structural homology in the form of a sterol-sensing domain, suggesting that release and sequestration of cholesterol-modified Hh may be based on related molecular pathways.
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