Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6719
pubmed:dateCreated
1999-2-25
pubmed:abstractText
The Drosophila eye, a paradigm for epithelial organization, is highly polarized with mirror-image symmetry about the equator. The R3 and R4 photoreceptors in each ommatidium are vital in this polarity; they adopt asymmetrical positions in adult ommatidia and are the site of action for several essential genes. Two such genes are frizzled (fz) and dishevelled (dsh), the products of which are components of a signalling pathway required in R3, and which are thought to be activated by a diffusible signal. Here we show that the transmembrane receptor Notch is required downstream of dsh in R3/R4 for them to adopt distinct fates. By using an enhancer for the Notch target gene Enhancer of split mdelta, we show that Notch becomes activated specifically in R4. We propose that Fz/Dsh promotes activity of the Notch ligand Delta and inhibits Notch receptor activity in R3, creating a difference in Notch signalling capacity between R3 and R4. Subsequent feedback in the Notch pathway ensures that this difference becomes amplified. This interplay between Fz/Dsh and Notch indicates that polarity is established through local comparisons between two cells and explains how a signal from one position (for example, the equator in the eye) could be interpreted by all ommatidia in the field.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Basic Helix-Loop-Helix..., http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/E(spl) region transcript mdelta..., http://linkedlifedata.com/resource/pubmed/chemical/Frizzled Receptors, http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Notch, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/dishevelled proteins, http://linkedlifedata.com/resource/pubmed/chemical/fz protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/notch protein, Drosophila
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
397
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
526-30
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10028969-Adaptor Proteins, Signal Transducing, pubmed-meshheading:10028969-Animals, pubmed-meshheading:10028969-Animals, Genetically Modified, pubmed-meshheading:10028969-Basic Helix-Loop-Helix Transcription Factors, pubmed-meshheading:10028969-Cell Lineage, pubmed-meshheading:10028969-Cell Polarity, pubmed-meshheading:10028969-DNA-Binding Proteins, pubmed-meshheading:10028969-Drosophila, pubmed-meshheading:10028969-Drosophila Proteins, pubmed-meshheading:10028969-Frizzled Receptors, pubmed-meshheading:10028969-Insect Proteins, pubmed-meshheading:10028969-Membrane Proteins, pubmed-meshheading:10028969-Phosphoproteins, pubmed-meshheading:10028969-Photoreceptor Cells, Invertebrate, pubmed-meshheading:10028969-Receptors, G-Protein-Coupled, pubmed-meshheading:10028969-Receptors, Notch, pubmed-meshheading:10028969-Repressor Proteins, pubmed-meshheading:10028969-Signal Transduction
pubmed:year
1999
pubmed:articleTitle
Frizzled regulation of Notch signalling polarizes cell fate in the Drosophila eye.
pubmed:affiliation
Department of Anatomy, University of Cambridge, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't