ArticleThe Journal of biological chemistry2013
Drosophila heparan sulfate 6-O-endosulfatase Sulf1 facilitates wingless (Wg) protein degradation.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- Discovery of a Functional Sequon for Chondroitin Sulfate Glycosylation.Research square · 2026Article
- In vivo activities of heparan sulfate differentially modified by NDSTs during development.Proteoglycan research · 2024Article
- New Insights into theJournal of agricultural and food chemistry · 2023Review
- Regulation of morphogen pathways by a Drosophila chondroitin sulfate proteoglycan Windpipe.Journal of cell science · 2023Article
- Molecular Genetic Techniques for the Proteoglycan Functions in Drosophila.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Endogenous epitope tagging of a JAK/STAT ligand Unpaired1 inmicroPublication biology · 2021Article
- Chondroitin sulfate proteoglycan Windpipe modulates Hedgehog signaling inMolecular biology of the cell · 2020Article
- Functional analysis of glycosylation using Drosophila melanogaster.Glycoconjugate journal · 2020Review
- Establishment and characterization of Drosophila cell lines mutant for heparan sulfate modifying enzymes.Glycobiology · 2019Article
- Loss of heparan sulfate in the niche leads to tumor-like germ cell growth in the Drosophila testis.Glycobiology · 2018Article
- Downregulation of HS6ST2 by miR-23b-3p enhances matrix degradation through p38 MAPK pathway in osteoarthritis.Cell death & disease · 2018Article
- Deciphering functional glycosaminoglycan motifs in development.Current opinion in structural biology · 2018Review
- Drosophila Sulf1 is required for the termination of intestinal stem cell division during regeneration.Journal of cell science · 2017Article
- The role of heparan sulphate in development: the ectodermal story.International journal of experimental pathology · 2016Review
- Heparan sulfate regulates the number and centrosome positioning of Drosophila male germline stem cells.Molecular biology of the cell · 2016Article
- Syndecan defines precise spindle orientation by modulating Wnt signaling in C. elegans.Development (Cambridge, England) · 2014Article
- Differential responses to Wnt and PCP disruption predict expression and developmental function of conserved and novel genes in a cnidarian.PLoS genetics · 2014Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Heparan sulfate proteoglycans regulate various physiological and developmental processes through interactions with a number of protein ligands. Heparan sulfate (HS)-ligand binding depends on the amount and patterns of sulfate groups on HS, which are controlled by various HS sulfotransferases in the Golgi apparatus as well as extracellular 6-O-endosulfatases called "Sulfs." Sulfs are a family of secreted molecules that specifically remove 6-O-sulfate groups within the highly sulfated regions on HS. Vertebrate Sulfs promote Wnt signaling, whereas the only Drosophila homologue of Sulfs, Sulf1, negatively regulates Wingless (Wg) signaling. To understand the molecular mechanism for the negative regulation of Wg signaling by Sulf1, we studied the effects of Sulf1 on HS-Wg interaction and Wg stability. Sulf1 overexpression strongly inhibited the binding of Wg to Dally, a potential target heparan sulfate proteoglycan of Sulf1. This effect of Drosophila Sulf1 on the HS-Wg interaction is similar to that of vertebrate Sulfs. Using in vitro, in vivo, and ex vivo systems, we show that Sulf1 reduces extracellular Wg protein levels, at least partly by facilitating Wg degradation. In addition, expression of human Sulf1 in the Drosophila wing disc lowers the levels of extracellular Wg protein, as observed for Drosophila Sulf1. Our study demonstrates that vertebrate and Drosophila Sulfs have an intrinsically similar activity and that the function of Sulfs in the fate of Wnt/Wg ligands is context-dependent.
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