@article {843291,
	title = {Dally cooperates with Drosophila Frizzled 2 to transduce Wingless signalling.},
	journal = {Nature},
	volume = {400},
	number = {6741},
	year = {1999},
	month = {1999 Jul 15},
	pages = {281-4},
	abstract = {
	The Drosophila wingless gene (wg) encodes a protein of the Wnt family and is a critical regulator in many developmental processes. Biochemical studies have indicated that heparan sulphate proteoglycans, consisting of a protein core to which heparan sulphate glycosaminoglycans are attached, are important for Wg function. Here we show that, consistent with these findings, the Drosophila gene sulfateless (sfl), which encodes a homologue of vertebrate heparan sulphate N-deacetylase/N-sulphotransferase (an enzyme needed for the modification of heparan sulphate) is essential for Wg signalling. We have identified the product of division abnormally delayed (dally), a glycosyl-phosphatidyl inositol (GPI)-linked glypican, as a heparan sulphate proteoglycan molecule involved in Wg signalling. Our results indicate that Dally may act as a co-receptor for Wg, and that Dally, together with Drosophila Frizzled 2, modulates both short- and long-range activities of Wg.

},
	keywords = {Amidohydrolases, Amino Acid Sequence, Animals, Body Patterning, Drosophila, Drosophila Proteins, Female, Frizzled Receptors, Genes, Insect, Heparin, Insect Proteins, Membrane Glycoproteins, Molecular Sequence Data, Mutation, Proteoglycans, Proto-Oncogene Proteins, Receptors, G-Protein-Coupled, Receptors, Neurotransmitter, Sequence Homology, Amino Acid, Signal Transduction, Sulfotransferases, Wings, Animal, Wnt1 Protein},
	issn = {0028-0836},
	doi = {10.1038/22343},
	author = {Lin, X and Perrimon, N}
}
