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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
2004-12-28
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pubmed:abstractText |
Ligand-induced proteolytic cleavage and internalization of the plasma membrane receptor Notch leads to its activation. Ligand-independent, steady-state internalization of Notch, however, does not lead to activation. The mechanism by which downstream effectors discriminate between these bipartite modes of Notch internalization is not understood. Nedd4 is a HECT domain-containing E3 ubiquitin ligase that targets transmembrane receptors containing the PPSY motif for endocytosis. Deltex is a positive Notch signaling regulator that encodes a putative ubiquitin ligase of the ring finger type.
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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/Cut protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Endosomal Sorting Complexes...,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nedd4 ubiquitin protein ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Notch,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/delta protein,
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 |
Dec
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pubmed:issn |
0960-9822
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2228-36
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15620649-Animals,
pubmed-meshheading:15620649-Cells, Cultured,
pubmed-meshheading:15620649-Drosophila,
pubmed-meshheading:15620649-Drosophila Proteins,
pubmed-meshheading:15620649-Endocytosis,
pubmed-meshheading:15620649-Endosomal Sorting Complexes Required for Transport,
pubmed-meshheading:15620649-Gene Expression Regulation,
pubmed-meshheading:15620649-Homeodomain Proteins,
pubmed-meshheading:15620649-Immunohistochemistry,
pubmed-meshheading:15620649-Immunoprecipitation,
pubmed-meshheading:15620649-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:15620649-Membrane Proteins,
pubmed-meshheading:15620649-Models, Biological,
pubmed-meshheading:15620649-Nerve Tissue Proteins,
pubmed-meshheading:15620649-Nuclear Proteins,
pubmed-meshheading:15620649-Protein Transport,
pubmed-meshheading:15620649-RNA Interference,
pubmed-meshheading:15620649-Receptors, Notch,
pubmed-meshheading:15620649-Signal Transduction,
pubmed-meshheading:15620649-Transcription Factors,
pubmed-meshheading:15620649-Ubiquitin,
pubmed-meshheading:15620649-Ubiquitin-Protein Ligases,
pubmed-meshheading:15620649-Wing
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pubmed:year |
2004
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pubmed:articleTitle |
Drosophila Nedd4 regulates endocytosis of notch and suppresses its ligand-independent activation.
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pubmed:affiliation |
RIKEN Center for Developmental Biology, Chuo-ku, Kobe 650-0047, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study
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