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Gene Review

dally  -  division abnormally delayed

Drosophila melanogaster

Synonyms: CG4974, CT15952, Dally, Dally protein, Division abnormally delayed protein, ...
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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


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].


  1. Drosophila Dpp morphogen movement is independent of dynamin-mediated endocytosis but regulated by the glypican members of heparan sulfate proteoglycans. Belenkaya, T.Y., Han, C., Yan, D., Opoka, R.J., Khodoun, M., Liu, H., Lin, X. Cell (2004) [Pubmed]
  2. Dally cooperates with Drosophila Frizzled 2 to transduce Wingless signalling. Lin, X., Perrimon, N. Nature (1999) [Pubmed]
  3. Hox control of morphogen mobility and organ development through regulation of glypican expression. Crickmore, M.A., Mann, R.S. Development (2007) [Pubmed]
  4. Dally regulates Dpp morphogen gradient formation in the Drosophila wing. Fujise, M., Takeo, S., Kamimura, K., Matsuo, T., Aigaki, T., Izumi, S., Nakato, H. Development (2003) [Pubmed]
  5. dally, a Drosophila member of the glypican family of integral membrane proteoglycans, affects cell cycle progression and morphogenesis via a Cyclin A-mediated process. Nakato, H., Fox, B., Selleck, S.B. J. Cell. Sci. (2002) [Pubmed]
  6. The function of a Drosophila glypican does not depend entirely on heparan sulfate modification. Kirkpatrick, C.A., Knox, S.M., Staatz, W.D., Fox, B., Lercher, D.M., Selleck, S.B. Dev. Biol. (2006) [Pubmed]
  7. The division abnormally delayed (dally) gene: a putative integral membrane proteoglycan required for cell division patterning during postembryonic development of the nervous system in Drosophila. Nakato, H., Futch, T.A., Selleck, S.B. Development (1995) [Pubmed]
  8. Expression of the cell surface proteoglycan glypican-5 is developmentally regulated in kidney, limb, and brain. Saunders, S., Paine-Saunders, S., Lander, A.D. Dev. Biol. (1997) [Pubmed]
  9. The glypican Dally-like is required for Hedgehog signalling in the embryonic epidermis of Drosophila. Desbordes, S.C., Sanson, B. Development (2003) [Pubmed]
  10. Regulation of dally, an integral membrane proteoglycan, and its function during adult sensory organ formation of Drosophila. Fujise, M., Izumi, S., Selleck, S.B., Nakato, H. Dev. Biol. (2001) [Pubmed]
  11. Drosophila glypicans Dally and Dally-like shape the extracellular Wingless morphogen gradient in the wing disc. Han, C., Yan, D., Belenkaya, T.Y., Lin, X. Development (2005) [Pubmed]
  12. Expression of a secreted form of Dally, a Drosophila glypican, induces overgrowth phenotype by affecting action range of Hedgehog. Takeo, S., Akiyama, T., Firkus, C., Aigaki, T., Nakato, H. Dev. Biol. (2005) [Pubmed]
  13. A screen for genes regulating the wingless gradient in Drosophila embryos. Desbordes, S.C., Chandraratna, D., Sanson, B. Genetics (2005) [Pubmed]
  14. Glypican LON-2 Is a Conserved Negative Regulator of BMP-like Signaling in Caenorhabditis elegans. Gumienny, T.L., Macneil, L.T., Wang, H., de Bono, M., Wrana, J.L., Padgett, R.W. Curr. Biol. (2007) [Pubmed]
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