| http://purl.uniprot.org/citations/10799545 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10799545 | http://www.w3.org/2000/01/rdf-schema#comment | "The Lck tyrosine kinase is involved in signaling by T cell surface receptors such as TCR/CD3, CD2, and CD28. As other downstream protein-tyrosine kinases are activated upon stimulation of these receptors, it is difficult to assign which tyrosine-phosphorylated proteins represent bona fide Lck substrates and which are phosphorylated by other tyrosine kinases. We have developed a system in which Lck can be activated independently of TCR/CD3. We have shown that activation of an epidermal growth factor receptor/Lck chimera leads to the specific phosphorylation of Ras GTPase-activating protein (RasGAP) and two RasGAP-associated proteins, p56(dok) and p62(dok). Activation of the chimeric protein correlates with an increase in cellular Ca(2+) in the absence of ZAP-70 and phospholipase Cgamma1 phosphorylation. Furthermore, we have found that p62(dok) co-immunoprecipitates with the activated epidermal growth factor receptor/LckF505 and that phosphorylated Dok proteins bind to the Src homology 2 domain of Lck in vitro. In addition, we have shown that activation via the CD2 but not the TCR/CD3 receptor leads to the phosphorylation of p56(dok) and p62(dok). Using JCaM1.6 cells, we have demonstrated that Lck is required for CD2-mediated phosphorylation of Dok proteins. We propose that phosphorylation and Src homology 2-mediated association of p56(dok) and p62(dok) with Lck play a selective function in accessory receptor signal transduction mechanisms."xsd:string |
| http://purl.uniprot.org/citations/10799545 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.275.19.14590"xsd:string |
| http://purl.uniprot.org/citations/10799545 | http://purl.uniprot.org/core/author | "Duplay P."xsd:string |
| http://purl.uniprot.org/citations/10799545 | http://purl.uniprot.org/core/author | "Nemorin J.G."xsd:string |
| http://purl.uniprot.org/citations/10799545 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10799545 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/10799545 | http://purl.uniprot.org/core/pages | "14590-14597"xsd:string |
| http://purl.uniprot.org/citations/10799545 | http://purl.uniprot.org/core/title | "Evidence that Llck-mediated phosphorylation of p56dok and p62dok may play a role in CD2 signaling."xsd:string |
| http://purl.uniprot.org/citations/10799545 | http://purl.uniprot.org/core/volume | "275"xsd:string |
| http://purl.uniprot.org/citations/10799545 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10799545 |
| http://purl.uniprot.org/citations/10799545 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10799545 |
| http://purl.uniprot.org/uniprot/O60496#attribution-9BF742A093F774392CE0F91FC2CB75A4 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/10799545 |
| http://purl.uniprot.org/uniprot/Q99704#attribution-9BF742A093F774392CE0F91FC2CB75A4 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/10799545 |
| http://purl.uniprot.org/uniprot/P37198#attribution-F31AAF456C8D7D355E65A029B51EFF9F | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/10799545 |