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Gene Review

sfl  -  sulfateless

Drosophila melanogaster

Synonyms: Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase, CG8339, CT24567, Dmel\CG8339, Glucosaminyl N-deacetylase/N-sulfotransferase, ...
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High impact information on sfl

  • 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 [1].
  • Mutations in this gene, which we call slalom, display defects in Wg and Hh signaling, which are likely due to the lack of sulfation of glycosaminoglycans by the sulfotransferase sulfateless [2].
  • Whereas the glycosylation and function of NOTCH are affected in imaginal disks of frc mutants, those of SPI and of GAG core proteins are not, even though FRC transports a broad range of glycosylation substrates, suggesting that Golgi units containing FRC and those containing SFL or RHO are functionally separable [3].
  • The UDP-sugar transporter FRINGE-CONNECTION (FRC) is localized to a subset of the Golgi units distinct from those harboring SULFATELESS (SFL), which modifies glucosaminoglycans (GAGs), and from those harboring the protease RHOMBOID (RHO), which processes the glycoprotein SPITZ (SPI) [3].
  • The Drosophila sugarless and sulfateless genes encode enzymes required for the biosynthesis of heparan sulfate glycosaminoglycans [4].

Associations of sfl with chemical compounds

  • Studies of mutations in the genes sugarless(sgl) and sulfateless (sfl) have proved that the proteoglycans involved in Wg signalling contain heparan sulfate GAG chains (Development 124 (1997) 2623; Development 124 (1997) 3055; Development 124 (1997) 3565; Development 126 (1999) 3715) [5].
  • Defects in sulfateless, a gene encoding a protein with similarity to vertebrate N-deacetylase/N-sulfotransferases, do not affect chondroitin sulfate levels or composition but dramatically alter the composition of heparin lyase-released disaccharides [6].

Other interactions of sfl

  • Structural analysis of glycosaminoglycans in animals bearing mutations in sugarless, sulfateless, and tout-velu. Drosophila homologues of vertebrate genes encoding glycosaminoglycan biosynthetic enzymes [6].


  1. Dally cooperates with Drosophila Frizzled 2 to transduce Wingless signalling. Lin, X., Perrimon, N. Nature (1999) [Pubmed]
  2. Slalom encodes an adenosine 3'-phosphate 5'-phosphosulfate transporter essential for development in Drosophila. Lüders, F., Segawa, H., Stein, D., Selva, E.M., Perrimon, N., Turco, S.J., Häcker, U. EMBO J. (2003) [Pubmed]
  3. Distinct functional units of the Golgi complex in Drosophila cells. Yano, H., Yamamoto-Hino, M., Abe, M., Kuwahara, R., Haraguchi, S., Kusaka, I., Awano, W., Kinoshita-Toyoda, A., Toyoda, H., Goto, S. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  4. Heparan sulfate proteoglycans are essential for FGF receptor signaling during Drosophila embryonic development. Lin, X., Buff, E.M., Perrimon, N., Michelson, A.M. Development (1999) [Pubmed]
  5. Dally-like protein, a new Drosophila glypican with expression overlapping with wingless. Khare, N., Baumgartner, S. Mech. Dev. (2000) [Pubmed]
  6. Structural analysis of glycosaminoglycans in animals bearing mutations in sugarless, sulfateless, and tout-velu. Drosophila homologues of vertebrate genes encoding glycosaminoglycan biosynthetic enzymes. Toyoda, H., Kinoshita-Toyoda, A., Fox, B., Selleck, S.B. J. Biol. Chem. (2000) [Pubmed]
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