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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2000-4-26
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pubmed:abstractText |
Endocytosis of the ligand delta; is required for activation of the receptor Notch during Drosophila development. The Notch extracellular domain (NotchECD) dissociates from the Notch intracellular domain (NotchICD) and is trans-endocytosed into delta;-expressing cells in wild-type imaginal discs. Reduction of dynamin-mediated endocytosis in developing eye and wing imaginal discs reduces Notch dissociation and Notch signalling. Furthermore, dynamin-mediated delta endocytosis is required for Notch trans-endocytosis in Drosophila cultured cell lines. Endocytosis-defective delta proteins fail to mediate trans-endocytosis of Notch in cultured cells, and exhibit aberrant subcellular trafficking and reduced signalling capacity in Drosophila. We suggest that endocytosis into delta-expressing cells of NotchECD bound to delta plays a critical role during activation of the Notch receptor and is required to achieve processing and dissociation of the Notch protein.
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pubmed:grant |
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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/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dynamins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Notch,
http://linkedlifedata.com/resource/pubmed/chemical/delta protein,
http://linkedlifedata.com/resource/pubmed/chemical/notch protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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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 |
127
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1373-85
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10704384-Animals,
pubmed-meshheading:10704384-Animals, Genetically Modified,
pubmed-meshheading:10704384-Base Sequence,
pubmed-meshheading:10704384-Cell Line,
pubmed-meshheading:10704384-DNA Primers,
pubmed-meshheading:10704384-Drosophila,
pubmed-meshheading:10704384-Drosophila Proteins,
pubmed-meshheading:10704384-Dynamins,
pubmed-meshheading:10704384-Endocytosis,
pubmed-meshheading:10704384-GTP Phosphohydrolases,
pubmed-meshheading:10704384-Genes, Insect,
pubmed-meshheading:10704384-Insect Proteins,
pubmed-meshheading:10704384-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10704384-Ligands,
pubmed-meshheading:10704384-Membrane Proteins,
pubmed-meshheading:10704384-Mutation,
pubmed-meshheading:10704384-Receptors, Notch,
pubmed-meshheading:10704384-Retina,
pubmed-meshheading:10704384-Signal Transduction,
pubmed-meshheading:10704384-Wing
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pubmed:year |
2000
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pubmed:articleTitle |
Ligand endocytosis drives receptor dissociation and activation in the Notch pathway.
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pubmed:affiliation |
Department of Biology, Indiana University, Bloomington, IN 47405, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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