| pubmed-article:16046028 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16046028 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
| pubmed-article:16046028 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:16046028 | lifeskim:mentions | umls-concept:C1413898 | lld:lifeskim |
| pubmed-article:16046028 | lifeskim:mentions | umls-concept:C0597358 | lld:lifeskim |
| pubmed-article:16046028 | lifeskim:mentions | umls-concept:C2266866 | lld:lifeskim |
| pubmed-article:16046028 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:16046028 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:16046028 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:16046028 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:16046028 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16046028 | pubmed:dateCreated | 2005-9-20 | lld:pubmed |
| pubmed-article:16046028 | pubmed:abstractText | Reelin-stimulated tyrosine phosphorylation of the Dab1 adaptor protein is required during brain development for Reelin-dependent neuron positioning in the cerebral cortex and various other laminated regions. Dab1 contains an amino-terminal PTB/PI domain through which it can bind to Reelin receptors and membrane phosphoinositides. The relative contributions of these binding activities were unknown. Here, we identify a mutation in the PTB domain of Dab1 that inhibits membrane localization without inhibiting receptor binding. In neurons, this mutation reduces both basal and Reelin-stimulated Dab1 tyrosine phosphorylation. In contrast, a mutation that inhibits receptor binding reduces Reelin-stimulated but not basal tyrosine phosphorylation. These results support a model in which phospholipids recruit Dab1 to membranes but do not play a direct role in relaying the Reelin signal, while direct Dab1-receptor interaction is responsible for relaying the Reelin signal but not for membrane recruitment. | lld:pubmed |
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| pubmed-article:16046028 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16046028 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16046028 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16046028 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16046028 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16046028 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:16046028 | pubmed:issn | 0169-328X | lld:pubmed |
| pubmed-article:16046028 | pubmed:author | pubmed-author:XuMeiM | lld:pubmed |
| pubmed-article:16046028 | pubmed:author | pubmed-author:CooperJonatha... | lld:pubmed |
| pubmed-article:16046028 | pubmed:author | pubmed-author:ArnaudLionelL | lld:pubmed |
| pubmed-article:16046028 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16046028 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:16046028 | pubmed:volume | 139 | lld:pubmed |
| pubmed-article:16046028 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16046028 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16046028 | pubmed:pagination | 300-5 | lld:pubmed |
| pubmed-article:16046028 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
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