High impact information on dally

• Furthermore, we show that Dpp fails to move across cells mutant for dally and dally-like (dly), two Drosophila glypican members of heparin sulfate proteoglycan (HSPG) [1].
• 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 [2].
• Compared with the serially homologous wing, where Ubx is not expressed, low levels of posterior dally in the haltere contribute to a reduced P compartment size and an overall smaller appendage size [3].
• Ubx, in combination with the posterior selector gene engrailed (en), represses dally expression in the posterior (P) compartment of the haltere [3].
• Dpp is a heparin-binding protein and Dpp signal transduction is potentiated by Dally, a cell-surface heparan sulfate proteoglycan, during assembly of several adult tissues [4].

Biological context of dally

• We have investigated the molecular basis of dally-mediated cell division defects by examining the genetic interactions between dally and known cell cycle regulators [5].
• Expression of HS-deficient Dally in vivo showed it does not promote signaling as well as wild-type Dally, yet it can rescue several dally mutant phenotypes [6].
• Given that Dally is known to regulate the activity of secreted growth factors our findings suggest that extracellular cues influence the degradation of Cyclin A in a manner that controls cell cycle progression and ultimately, cell division patterning [5].
• The division abnormally delayed (dally) locus was identified using a combination of "enhancer trap" and behavioral screening methods [7].
• Although little is known about functional differences between individual members of the glypican gene family, mutations in both the Drosophila gene dally and the human gene for glypican-3 strongly suggest that at least some glypicans do function in cellular growth control and morphogenesis [8].

Anatomical context of dally

• The Drosophila genes dally and dally-like encode glypicans, which are heparan sulphate proteoglycans anchored to the cell membrane by a glycosylphosphatidylinositol link [9].
• The ordered cell cycle progression of lamina precursor cells, which generate synaptic target neurons for photoreceptors, is disrupted in dally mutants [7].

Associations of dally with chemical compounds

• These data reveal that heparan sulfate modification of Dally is not required for all in vivo activities and that significant functional capacity resides in the protein core [6].

Physical interactions of dally

• Cell binding and co-immunoprecipitation studies suggest that non-HS-modified Dally retains some ability to bind Dpp or BMP4 [6].

Regulatory relationships of dally

• These findings suggest that dally can differentially regulate Wg- or Dpp-directed patterning during sensory organ assembly [10].
• Dally regulates Dpp morphogen gradient formation in the Drosophila wing [4].

Other interactions of dally

• dally, a Drosophila member of the glypican family of integral membrane proteoglycans, affects cell cycle progression and morphogenesis via a Cyclin A-mediated process [5].
• FGF binding is abolished by preincubation with HS, but BMP4 association is partially HS-resistant, suggesting the Dally protein core contributes to binding [6].
• Last, we demonstrate that Wg movement is impeded by cells mutant for both dally and dlp [11].
• Expression of a secreted form of Dally, a Drosophila glypican, induces overgrowth phenotype by affecting action range of Hedgehog [12].
• After using a secondary screen to test for mutants and smaller deficiencies, we identified three interacting genes: dally, notum, and brahma [13].

Analytical, diagnostic and therapeutic context of dally

• To understand the functional contributions of HS chains and protein core we have (1) assessed the growth factor binding properties of purified Dally using surface plasmon resonance, (2) generated a form of Dally that is not HS modified and evaluated its signaling capacity in vivo [6].
• LON-2 is functionally conserved because the Drosophila glypican gene dally rescues the lon-2(lf) body-size defect [14].

References