pubmed-article:15286081 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15286081 | lifeskim:mentions | umls-concept:C0086282 | lld:lifeskim |
pubmed-article:15286081 | lifeskim:mentions | umls-concept:C0085103 | lld:lifeskim |
pubmed-article:15286081 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
pubmed-article:15286081 | lifeskim:mentions | umls-concept:C1420393 | lld:lifeskim |
pubmed-article:15286081 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:15286081 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:15286081 | pubmed:issue | 40 | lld:pubmed |
pubmed-article:15286081 | pubmed:dateCreated | 2004-9-27 | lld:pubmed |
pubmed-article:15286081 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15286081 | pubmed:abstractText | Activation of Ret, the receptor-tyrosine kinase for the glial cell line-derived neurotrophic factor (GDNF) family ligands (GFLs), results in the recruitment and assembly of adaptor protein complexes that function to transduce signals downstream of the receptor. Here we identify Dok-6, a novel member of the Dok-4/5 subclass of the p62 Dok family of intracellular adaptor molecules, and characterize its interaction with Ret. Expression analysis reveals that Dok-6 is highly expressed in the developing central nervous system and is co-expressed with Ret in several locations, including sympathetic, sensory, and parasympathetic ganglia, as well as in the ureteric buds of the developing kidneys. Pull-down assays using the Dok-6 phosphotyrosine binding (PTB) domain and GDNF-activated Ret indicate that Dok-6 binds to the phosphorylated Ret Tyr(1062) residue. Moreover, ligand activation of Ret resulted in phosphorylation of tyrosine residue(s) located within the unique C terminus of Dok-6 predominantly through a Src-dependent mechanism, indicating that Dok-6 is a substrate of the Ret-Src signaling pathway. Interestingly, expression of Dok-6 potentiated GDNF-induced neurite outgrowth in GDNF family receptor alpha1 (GFRalpha1)-expressing Neuro2A cells that was dependent upon the C-terminal residues of Dok-6. Taken together, these data identify Dok-6 as a novel Dok-4/5-related adaptor molecule that may function in vivo to transduce signals that regulate Ret-mediated processes such as axonal projection. | lld:pubmed |
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pubmed-article:15286081 | pubmed:language | eng | lld:pubmed |
pubmed-article:15286081 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15286081 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15286081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:15286081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15286081 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15286081 | pubmed:month | Oct | lld:pubmed |
pubmed-article:15286081 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:15286081 | pubmed:author | pubmed-author:YangMaoM | lld:pubmed |
pubmed-article:15286081 | pubmed:author | pubmed-author:JohnsonEugene... | lld:pubmed |
pubmed-article:15286081 | pubmed:author | pubmed-author:MilbrandtJeff... | lld:pubmed |
pubmed-article:15286081 | pubmed:author | pubmed-author:CrowderRobert... | lld:pubmed |
pubmed-article:15286081 | pubmed:author | pubmed-author:EnomotoHideki... | lld:pubmed |
pubmed-article:15286081 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15286081 | pubmed:day | 1 | lld:pubmed |
pubmed-article:15286081 | pubmed:volume | 279 | lld:pubmed |
pubmed-article:15286081 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15286081 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15286081 | pubmed:pagination | 42072-81 | lld:pubmed |
pubmed-article:15286081 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:15286081 | pubmed:meshHeading | pubmed-meshheading:15286081... | lld:pubmed |
pubmed-article:15286081 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15286081 | pubmed:articleTitle | Dok-6, a Novel p62 Dok family member, promotes Ret-mediated neurite outgrowth. | lld:pubmed |
pubmed-article:15286081 | pubmed:affiliation | Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, Missouri 63110, USA. | lld:pubmed |
pubmed-article:15286081 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15286081 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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