Source:http://linkedlifedata.com/resource/pubmed/id/12403719
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
23
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| pubmed:dateCreated |
2002-10-29
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| pubmed:databankReference | |
| pubmed:abstractText |
The C. elegans genome encodes a single Eph receptor tyrosine kinase, VAB-1, which functions in neurons to control epidermal morphogenesis. Four members of the ephrin family of ligands for Eph receptors have been identified in C. elegans. Three ephrins (EFN-1/VAB-2, EFN-2 and EFN-3) have been previously shown to function in VAB-1 signaling. We show that mutations in the gene mab-26 affect the fourth C. elegans ephrin, EFN-4. We show that efn-4 also functions in embryonic morphogenesis, and that it is expressed in the developing nervous system. Interestingly, efn-4 mutations display synergistic interactions with mutations in the VAB-1 receptor and in the EFN-1 ephrin, indicating that EFN-4 may function independently of the VAB-1 Eph receptor in morphogenesis. Mutations in the LAR-like receptor tyrosine phosphatase PTP-3 and in the Semaphorin-2A homolog MAB-20 disrupt embryonic neural morphogenesis. efn-4 mutations synergize with ptp-3 mutations, but not with mab-20 mutations, suggesting that EFN-4 and Semaphorin signaling could function in a common pathway or in opposing pathways in C. elegans embryogenesis.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ephrins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/mab-20 protein, C elegans
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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 |
129
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
5499-510
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:12403719-Amino Acid Sequence,
pubmed-meshheading:12403719-Animals,
pubmed-meshheading:12403719-Caenorhabditis elegans,
pubmed-meshheading:12403719-Caenorhabditis elegans Proteins,
pubmed-meshheading:12403719-Cell Cycle Proteins,
pubmed-meshheading:12403719-Ephrins,
pubmed-meshheading:12403719-Epistasis, Genetic,
pubmed-meshheading:12403719-Genes, Reporter,
pubmed-meshheading:12403719-Humans,
pubmed-meshheading:12403719-Larva,
pubmed-meshheading:12403719-Male,
pubmed-meshheading:12403719-Membrane Proteins,
pubmed-meshheading:12403719-Molecular Sequence Data,
pubmed-meshheading:12403719-Morphogenesis,
pubmed-meshheading:12403719-Mutation,
pubmed-meshheading:12403719-Nerve Tissue Proteins,
pubmed-meshheading:12403719-Nervous System,
pubmed-meshheading:12403719-Organisms, Genetically Modified,
pubmed-meshheading:12403719-Sequence Alignment,
pubmed-meshheading:12403719-Signal Transduction
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| pubmed:year |
2002
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| pubmed:articleTitle |
The divergent C. elegans ephrin EFN-4 functions inembryonic morphogenesis in a pathway independent of the VAB-1 Eph receptor.
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| pubmed:affiliation |
Department of Molecular, Cell, and Developmental Biology, Sinsheimer Laboratories, University of California, Santa Cruz 95064, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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