Source:http://linkedlifedata.com/resource/pubmed/id/11861487
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2002-2-25
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pubmed:abstractText |
The Notch pathway is an evolutionarily conserved signaling mechanism that is essential for cell-cell interactions. The Drosophila deltex gene regulates Notch signaling in a positive manner, and its gene product physically interacts with the intracellular domain of Notch through its N-terminal domain. Deltex has two other domains that are presumably involved in protein-protein interactions: a proline-rich motif that binds to SH3-domains, and a RING-H2 finger motif. Using an overexpression assay, we have analyzed the functional involvement of these Deltex domains in Notch signaling. The N-terminal domain of Deltex that binds to the CDC10/Ankyrin repeats of the Notch intracellular domain was indispensable for the function of Deltex. A mutant form of Deltex that lacked the proline-rich motif behaved as a dominant-negative form. This dominant-negative Deltex inhibited Notch signaling upstream of an activated, nuclear form of Notch and downstream of full-length Notch, suggesting the dominant-negative Deltex might prevent the activation of the Notch receptor. We found that Deltex formed a homo-multimer, and mutations in the RING-H2 finger domain abolished this oligomerization. The same mutations in the RING-H2 finger motif of Deltex disrupted the function of Deltex in vivo. However, when the same mutant was fused to a heterologous dimerization domain (Glutathione-S-Transferase), the chimeric protein had normal Deltex activity. Therefore, oligomerization mediated by the RING-H2 finger motif is an integral step in the signaling function of Deltex.
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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/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Notch,
http://linkedlifedata.com/resource/pubmed/chemical/deltex protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/notch protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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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 |
1049-59
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11861487-Amino Acid Motifs,
pubmed-meshheading:11861487-Animals,
pubmed-meshheading:11861487-Animals, Genetically Modified,
pubmed-meshheading:11861487-Drosophila,
pubmed-meshheading:11861487-Drosophila Proteins,
pubmed-meshheading:11861487-Insect Proteins,
pubmed-meshheading:11861487-Membrane Proteins,
pubmed-meshheading:11861487-Mutagenesis,
pubmed-meshheading:11861487-Proline,
pubmed-meshheading:11861487-Receptors, Notch,
pubmed-meshheading:11861487-Signal Transduction
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pubmed:year |
2002
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pubmed:articleTitle |
Involvement of a proline-rich motif and RING-H2 finger of Deltex in the regulation of Notch signaling.
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pubmed:affiliation |
Department of Biological Science and Technology, Science University of Tokyo, 2641 Yamazaki, Noda, Chiba 278-8510, Japan. matsuno@rs.noda.sut.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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