| http://purl.uniprot.org/citations/11825908 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11825908 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11825908 | http://www.w3.org/2000/01/rdf-schema#comment | "Dok-1 is an adaptor protein that is a substrate for Bcr-Abl and other tyrosine protein kinases. The presence of pleckstrin homology and phosphotyrosine binding domains as well as multiple tyrosine phosphorylation sites suggests that Dok-1 is involved in protein-protein and/or protein-lipid interactions. Here we show that stimulation of Mo7 hematopoietic cells with c-Kit ligand (KL) induces phosphatidylinositol (PI) 3-kinase-dependent tyrosine phosphorylation and membrane recruitment of Dok-1. Addition of the K-Ras membrane-targeting motif to Dok-1 generated a constitutively membrane-bound Dok-1 protein whose tyrosine phosphorylation was independent of PI 3-kinase. Membrane localization of Dok-1 was required for its ability to function as a negative regulator of cell proliferation. Additional experiments revealed that Dok-1 associated with the juxtamembrane region and C-terminal tail of c-Kit. Lyn promoted phosphorylation of c-Kit and association of c-Kit and Dok-1. Both Lyn and Tec were capable of phosphorylating Dok-1. However, the use of primary bone marrow mast cells from normal and Lyn-deficient mice demonstrated that Lyn is required for KL-dependent Dok-1 tyrosine phosphorylation. Taken together, these data indicate that activation of PI 3-kinase by KL promotes binding of the Dok pleckstrin homology domain and Dok-1 recruitment to the plasma membrane where Dok-1 is phosphorylated by Src and/or Tec family kinases."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m200277200"xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m200277200"xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/author | "Liang X."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/author | "Liang X."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/author | "Clarkson B."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/author | "Clarkson B."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/author | "Strife A."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/author | "Strife A."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/author | "Wisniewski D."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/author | "Wisniewski D."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/author | "Resh M.D."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/author | "Resh M.D."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/author | "Shivakrupa R."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/author | "Shivakrupa R."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/pages | "13732-13738"xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/pages | "13732-13738"xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/title | "Phosphatidylinositol 3-kinase and Src family kinases are required for phosphorylation and membrane recruitment of Dok-1 in c-Kit signaling."xsd:string |
| http://purl.uniprot.org/citations/11825908 | http://purl.uniprot.org/core/title | "Phosphatidylinositol 3-kinase and Src family kinases are required for phosphorylation and membrane recruitment of Dok-1 in c-Kit signaling."xsd:string |