rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
12
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pubmed:dateCreated |
1996-3-11
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pubmed:abstractText |
The tissue polarity genes in Drosophila are required to coordinate cell polarity within the plane of the epidermis. Evidence to date suggests that these genes may encode components of a novel signal transduction pathway. Three of the genes, frizzled (fz), dishevelled (dsh), and prickle (pk) share a similar tissue polarity phenotype, suggesting that they function together in a single process. dsh is also known to function as a mediator of wingless (wg) signaling in a variety of developmental patterning processes in the fly. In this study, we make use of a fz transgene and a hypomorphic fz allele as genetic tools in an attempt to order these genes in a genetic hierarchy. Our results argue that dsh encodes a dosage sensitive component required for fz function and that it likely acts downstream of fz in the generation of tissue polarity. Our findings suggest that dsh may have a general role in signal transduction, perhaps as a component of a receptor complex.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Frizzled Receptors,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/dishevelled proteins,
http://linkedlifedata.com/resource/pubmed/chemical/fz protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0950-1991
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
121
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4095-102
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8575310-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:8575310-Animals,
pubmed-meshheading:8575310-Cell Polarity,
pubmed-meshheading:8575310-Drosophila,
pubmed-meshheading:8575310-Drosophila Proteins,
pubmed-meshheading:8575310-Epidermis,
pubmed-meshheading:8575310-Frizzled Receptors,
pubmed-meshheading:8575310-Genes, Insect,
pubmed-meshheading:8575310-Membrane Proteins,
pubmed-meshheading:8575310-Morphogenesis,
pubmed-meshheading:8575310-Mutation,
pubmed-meshheading:8575310-Phenotype,
pubmed-meshheading:8575310-Phosphoproteins,
pubmed-meshheading:8575310-Proteins,
pubmed-meshheading:8575310-Receptors, G-Protein-Coupled,
pubmed-meshheading:8575310-Signal Transduction,
pubmed-meshheading:8575310-Wing
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pubmed:year |
1995
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pubmed:articleTitle |
Dishevelled is a component of the frizzled signaling pathway in Drosophila.
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pubmed:affiliation |
Biology Department, University of Virginia, Charlottesville 22903, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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