The cell-surface proteoglycan Dally regulates Wingless signalling in Drosophila

Manabu Tsuda, Keisuke Kamimura, Hiroshi Nakato, Michael Archer, William Staatz, Bethany Fox, Melanie Humphrey, Sara Olson, Tracy Futch, Vesna Kaluza, Esther Siegfried, Lynn Stam and Scott B. Selleck ()
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Manabu Tsuda: Tokyo Metropolitan University
Keisuke Kamimura: Tokyo Metropolitan University
Hiroshi Nakato: Tokyo Metropolitan University
Michael Archer: University of Arizona
William Staatz: University of Arizona
Bethany Fox: University of Arizona
Melanie Humphrey: University of Arizona
Sara Olson: University of Arizona
Tracy Futch: University of Arizona
Vesna Kaluza: University of Arizona
Esther Siegfried: Pennsylvania State University
Lynn Stam: Novartis Inc.
Scott B. Selleck: University of Arizona

Nature, 1999, vol. 400, issue 6741, 276-280

Abstract: Abstract Wingless (Wg) is a member of the Wnt family of growth factors, secreted proteins that control proliferation and differentiation during development. Studies in Drosophila have shown that responses to Wg require cell-surface heparan sulphate, a glycosaminoglycan component of proteoglycans1,2,3,4. These findings suggest that a cell-surface proteoglycan is a component of a Wg/Wnt receptor complex. We demonstrate here that the protein encoded by the division abnormally delayed (dally) gene is a cell-surface, heparan-sulphate-modified proteoglycan5,6. dally partial loss-of-function mutations compromise Wg-directed events, and disruption of dally function with RNA interference produces phenotypes comparable to those found with RNA interference of wg or frizzled (fz)/Dfz2 (ref. 7). Ectopic expression of Dally potentiates Wg signalling without altering levels of Wg and can rescue a wg partial loss-of-function mutant. We also show that dally, a regulator of Decapentaplegic (Dpp) signalling during post-embryonic development, has tissue-specific effects on Wg and Dpp signalling. Dally can therefore differentially influence signalling mediated by two growth factors, and may form a regulatory component of both Wg and Dpp receptor complexes.

Date: 1999
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DOI: 10.1038/22336

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