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rdf:type |
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lifeskim:mentions |
umls-concept:C0013138,
umls-concept:C0037083,
umls-concept:C0061355,
umls-concept:C0079429,
umls-concept:C0086418,
umls-concept:C0162610,
umls-concept:C1334043,
umls-concept:C1416171,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1710082,
umls-concept:C1824662
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pubmed:issue |
5
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pubmed:dateCreated |
1996-6-21
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pubmed:databankReference |
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pubmed:abstractText |
The homologous receptors LIN-12 and GLP-1 mediate diverse cell-signaling events during development of the nematode Caenorhabditis elegans. These two receptors appear to be functionally interchangeable and have sequence similarity to Drosophila Notch. Here we focus on a molecular analysis of the lag-1 gene (lin-12 -and glp-1), which plays a central role in LIN-12 and GLP-1-mediated signal transduction. We find that the predicted LAG-1 protein is homologous to two DNA-binding proteins: human C Promoter Binding Factor (CBF1) and Drosophila Suppressor of Hairless (Su(H)). Furthermore, we show that LAG-1 binds specifically to the DNA sequence RTGGGAA, previously identified as a CBF-1/Su(H)-binding site. Finally, we report that the 5' flanking regions and first introns of the lin-12, glp-1 and lag-1 genes are enriched for potential LAG-1-binding sites. We propose that LAG-1 is a transcriptional regulator that serves as a primary link between the LIN-12 and GLP-1 receptors and downstream target genes in C. elegans. In addition, we propose that LAG-1 may be a key component of a positive feedback loop that amplifies activity of the LIN-12/GLP-1 pathway.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glp-1 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin J Recombination...,
http://linkedlifedata.com/resource/pubmed/chemical/Lin-12 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RBPJ protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/suppressor of Hairless protein...
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0950-1991
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
122
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1373-83
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pubmed:dateRevised |
2007-7-25
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pubmed:meshHeading |
pubmed-meshheading:8625826-Amino Acid Sequence,
pubmed-meshheading:8625826-Animals,
pubmed-meshheading:8625826-Base Sequence,
pubmed-meshheading:8625826-Caenorhabditis elegans,
pubmed-meshheading:8625826-Caenorhabditis elegans Proteins,
pubmed-meshheading:8625826-Chromosome Mapping,
pubmed-meshheading:8625826-Cloning, Molecular,
pubmed-meshheading:8625826-DNA-Binding Proteins,
pubmed-meshheading:8625826-Drosophila Proteins,
pubmed-meshheading:8625826-Genes, Helminth,
pubmed-meshheading:8625826-Helminth Proteins,
pubmed-meshheading:8625826-Humans,
pubmed-meshheading:8625826-Immunoglobulin J Recombination Signal Sequence-Binding...,
pubmed-meshheading:8625826-Membrane Glycoproteins,
pubmed-meshheading:8625826-Membrane Proteins,
pubmed-meshheading:8625826-Models, Biological,
pubmed-meshheading:8625826-Molecular Sequence Data,
pubmed-meshheading:8625826-Mutation,
pubmed-meshheading:8625826-Nuclear Proteins,
pubmed-meshheading:8625826-Polymerase Chain Reaction,
pubmed-meshheading:8625826-Protein Binding,
pubmed-meshheading:8625826-Repressor Proteins,
pubmed-meshheading:8625826-Sequence Analysis, DNA,
pubmed-meshheading:8625826-Sequence Homology, Amino Acid,
pubmed-meshheading:8625826-Signal Transduction
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pubmed:year |
1996
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pubmed:articleTitle |
lag-1, a gene required for lin-12 and glp-1 signaling in Caenorhabditis elegans, is homologous to human CBF1 and Drosophila Su(H).
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pubmed:affiliation |
Department of Genetics, University of Wisconsin-Madison 53706, USA.
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pubmed:publicationType |
Journal Article
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