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| pubmed-article:10704384 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:10704384 | lifeskim:mentions | umls-concept:C0014139 | lld:lifeskim |
| pubmed-article:10704384 | lifeskim:mentions | umls-concept:C0013126 | lld:lifeskim |
| pubmed-article:10704384 | lifeskim:mentions | umls-concept:C0086168 | lld:lifeskim |
| pubmed-article:10704384 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:10704384 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:10704384 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:10704384 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:10704384 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:10704384 | pubmed:dateCreated | 2000-4-26 | lld:pubmed |
| pubmed-article:10704384 | 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. | lld:pubmed |
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| pubmed-article:10704384 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10704384 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10704384 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10704384 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10704384 | pubmed:issn | 0950-1991 | lld:pubmed |
| pubmed-article:10704384 | pubmed:author | pubmed-author:MuskavitchM... | lld:pubmed |
| pubmed-article:10704384 | pubmed:author | pubmed-author:ParksA LAL | lld:pubmed |
| pubmed-article:10704384 | pubmed:author | pubmed-author:KluegK MKM | lld:pubmed |
| pubmed-article:10704384 | pubmed:author | pubmed-author:StoutJ RJR | lld:pubmed |
| pubmed-article:10704384 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10704384 | pubmed:volume | 127 | lld:pubmed |
| pubmed-article:10704384 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10704384 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10704384 | pubmed:pagination | 1373-85 | lld:pubmed |
| pubmed-article:10704384 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:10704384 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10704384 | pubmed:articleTitle | Ligand endocytosis drives receptor dissociation and activation in the Notch pathway. | lld:pubmed |
| pubmed-article:10704384 | pubmed:affiliation | Department of Biology, Indiana University, Bloomington, IN 47405, USA. | lld:pubmed |
| pubmed-article:10704384 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10704384 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10704384 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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