The function of a Drosophila glypican does not depend entirely on heparan sulfate modification.
作者： Catherine A. Kirkpatrick , Sarah M. Knox , William D. Staatz , Bethany Fox , Daniel M. Lercher
DOI: 10.1016/J.YDBIO.2006.09.011
关键词:
摘要: Division abnormally delayed (Dally) is one of two glycosylphosphatidylinositol (GPI)-linked heparan sulfate proteoglycans in Drosophila. Numerous studies have shown that it influences Decapentaplegic (Dpp) and Wingless signaling. It has been generally assumed Dally affects signaling by directly interacting with these growth factors, primarily through its (HS) chains. To understand the functional contributions HS chains protein core we (1) assessed factor binding properties purified using surface plasmon resonance, (2) generated a form not modified evaluated capacity vivo. Purified binds to FGF2, FGF10, Dpp homolog BMP4. FGF abolished preincubation HS, but BMP4 association partially HS-resistant, suggesting contributes binding. Cell co-immunoprecipitation suggest non-HS-modified retains some ability bind or Expression HS-deficient vivo showed does promote as well wild-type Dally, yet can rescue several dally mutant phenotypes. These data reveal modification required for all activities significant resides core.
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