| pubmed-article:1545818 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1545818 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:1545818 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:1545818 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:1545818 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:1545818 | pubmed:dateCreated | 1992-4-13 | lld:pubmed |
| pubmed-article:1545818 | pubmed:abstractText | The Src homology 2 (SH2) domain is a noncatalytic region which is conserved among a number of signaling and transforming proteins, including cytoplasmic protein-tyrosine kinases and Ras GTPase-activating protein (GAP). Genetic and biochemical data indicate that the SH2 domain of the p60v-src (v-Src) protein-tyrosine kinase is required for full v-src transforming activity and may direct the association of v-Src with specific tyrosine-phosphorylated proteins. To test the ability of the v-Src SH2 domain to mediate protein-protein interactions, v-Src polypeptides were expressed as fusion proteins in Escherichia coli. The bacterial v-Src SH2 domain bound a series of tyrosine-phosphorylated proteins in a lysate of v-src-transformed Rat-2 cells, including prominent species of 130 and 62 kDa (p130 and p62). The p130 and p62 tyrosine-phosphorylated proteins that complexed v-Src SH2 in vitro also associated with v-Src in v-src-transformed Rat-2 cells; this in vivo binding was dependent on the v-Src SH2 domain. In addition to binding soluble p62 and p130, the SH2 domains of v-Src, GAP, and v-Crk directly recognized these phosphotyrosine-containing proteins which had been previously denatured and immobilized on a filter. In addition, the SH2 domains of GAP and v-Crk bound to the GAP-associated protein p190 immobilized on a nitrocellulose membrane. These results show that SH2 domains bind directly to tyrosine-phosphorylated proteins and that the Src SH2 domain can bind phosphorylated targets of the v-Src kinase domain.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
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| pubmed-article:1545818 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1545818 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1545818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1545818 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1545818 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:1545818 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:1545818 | pubmed:author | pubmed-author:AndersonDD | lld:pubmed |
| pubmed-article:1545818 | pubmed:author | pubmed-author:PawsonTT | lld:pubmed |
| pubmed-article:1545818 | pubmed:author | pubmed-author:MoloyP JPJ | lld:pubmed |
| pubmed-article:1545818 | pubmed:author | pubmed-author:HULLR NRN | lld:pubmed |
| pubmed-article:1545818 | pubmed:author | pubmed-author:LiuX QXQ | lld:pubmed |
| pubmed-article:1545818 | pubmed:author | pubmed-author:MbamaluGG | lld:pubmed |
| pubmed-article:1545818 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1545818 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:1545818 | pubmed:geneSymbol | v-src | lld:pubmed |
| pubmed-article:1545818 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1545818 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1545818 | pubmed:pagination | 1366-74 | lld:pubmed |
| pubmed-article:1545818 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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