The four-jointed gene is required in the Drosophila eye for ommatidial polarity specification

Curr Biol. 1999 Dec 2;9(23):1363-72. doi: 10.1016/s0960-9822(00)80081-0.

Abstract

Background: The Drosophila eye is composed of about 800 ommatidia, each of which becomes dorsoventrally polarised in a process requiring signalling through the Notch, JAK/STAT and Wingless pathways. These three pathways are thought to act by setting up a gradient of a signalling molecule (or molecules) often referred to as the 'second signal'. Thus far, no candidate for a second signal has been identified.

Results: The four-jointed locus encodes a type II transmembrane protein that is expressed in a dorsoventral gradient in the developing eye disc. We have analysed the function and regulation of four-jointed during eye patterning. Loss-of-function clones or ectopic expression of four-jointed resulted in strong non-autonomous defects in ommatidial polarity on the dorsoventral axis. Ectopic expression experiments indicated that localised four-jointed expression was required at the time during development when ommatidial polarity was being determined. In contrast, complete removal of four-jointed function resulted in only a mild ommatidial polarity defect. Finally, we found that four-jointed expression was regulated by the Notch, JAK/STAT and Wingless pathways, consistent with it mediating their effects on ommatidial polarity.

Conclusions: The clonal phenotypes, time of requirement and regulation of four-jointed are consistent with it acting in ommatidial polarity determination as a second signal downstream of Notch, JAK/STAT and Wingless. Interestingly, it appears to act redundantly with unknown factors in this process, providing an explanation for the previous failure to identify a second signal.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Body Patterning / genetics*
  • Cloning, Molecular
  • DNA-Binding Proteins / metabolism
  • Drosophila / embryology*
  • Drosophila Proteins*
  • Eye / embryology*
  • Eye / metabolism
  • Frizzled Receptors
  • Insect Proteins / physiology*
  • Janus Kinase 3
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism
  • Membrane Glycoproteins / physiology*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Membrane Proteins / physiology
  • Microscopy, Confocal
  • Molecular Sequence Data
  • Mutation
  • Polymerase Chain Reaction
  • Protein-Tyrosine Kinases / metabolism
  • Proto-Oncogene Proteins / metabolism
  • Receptors, G-Protein-Coupled
  • Receptors, Notch
  • STAT1 Transcription Factor
  • Signal Transduction
  • Trans-Activators / metabolism
  • Wnt1 Protein

Substances

  • DNA-Binding Proteins
  • Drosophila Proteins
  • Frizzled Receptors
  • Insect Proteins
  • Membrane Glycoproteins
  • Membrane Proteins
  • N protein, Drosophila
  • Proto-Oncogene Proteins
  • Receptors, G-Protein-Coupled
  • Receptors, Notch
  • STAT1 Transcription Factor
  • Trans-Activators
  • Wnt1 Protein
  • fj protein, Drosophila
  • fz protein, Drosophila
  • wg protein, Drosophila
  • Protein-Tyrosine Kinases
  • Janus Kinase 3

Associated data

  • GENBANK/AC004295