| pubmed-article:11160680 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11160680 | lifeskim:mentions | umls-concept:C0000742 | lld:lifeskim |
| pubmed-article:11160680 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
| pubmed-article:11160680 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:11160680 | lifeskim:mentions | umls-concept:C0282534 | lld:lifeskim |
| pubmed-article:11160680 | lifeskim:mentions | umls-concept:C0679058 | lld:lifeskim |
| pubmed-article:11160680 | lifeskim:mentions | umls-concept:C1547699 | lld:lifeskim |
| pubmed-article:11160680 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
| pubmed-article:11160680 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
| pubmed-article:11160680 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:11160680 | pubmed:dateCreated | 2001-2-22 | lld:pubmed |
| pubmed-article:11160680 | pubmed:abstractText | Abelson murine leukemia virus (Ab-MLV) encodes the v-Abl protein tyrosine kinase and induces transformation of immortalized fibroblast lines and pre-B cells. Temperature-sensitive mutations affecting the kinase domain of the protein have demonstrated that the kinase activity is absolutely required for transformation. Despite this requirement, mutations affecting other regions of v-Abl modulate transformation activity. The SH2 domain and the highly conserved FLVRES motif within it form a phosphotyrosine-binding pocket that is required for interactions between the kinase and cellular substrates. To understand the impact of SH2 alterations on Ab-MLV-mediated transformation, we studied the Ab-MLV mutant P120/R273K. This mutant encodes a v-Abl protein in which the beta B5 arginine at the base of the phosphotyrosine-binding pocket has been replaced by a lysine. Unexpectedly, infection of NIH 3T3 or pre-B cells with P120/R273K revealed a temperature-dependent transformation phenotype. At 34 degrees C, P120/R273K transformed about 10-fold fewer cells than wild-type virus of equivalent titer; at 39.5 degrees C, 300-fold fewer NIH 3T3 cells were transformed and pre-B cells were refractory to transformation. Temperature-dependent transformation was accompanied by decreased phosphorylation of Shc, a protein that interacts with the v-Abl SH2 and links the protein to Ras, and decreased induction of c-Myc expression. These data suggest that alteration of the FLVRES pocket affects the ability of v-Abl to interact with at least some of its substrates in a temperature-dependent fashion and identify a novel type of temperature-sensitive Abelson virus. | lld:pubmed |
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| pubmed-article:11160680 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11160680 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11160680 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11160680 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11160680 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:11160680 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:11160680 | pubmed:author | pubmed-author:RosenbergNN | lld:pubmed |
| pubmed-article:11160680 | pubmed:author | pubmed-author:MainvilleC... | lld:pubmed |
| pubmed-article:11160680 | pubmed:author | pubmed-author:GoodPP | lld:pubmed |
| pubmed-article:11160680 | pubmed:author | pubmed-author:ParmarKK | lld:pubmed |
| pubmed-article:11160680 | pubmed:author | pubmed-author:RaffelG DGD | lld:pubmed |
| pubmed-article:11160680 | pubmed:author | pubmed-author:UnnikrishnanI... | lld:pubmed |
| pubmed-article:11160680 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11160680 | pubmed:volume | 75 | lld:pubmed |
| pubmed-article:11160680 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11160680 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11160680 | pubmed:pagination | 1816-23 | lld:pubmed |
| pubmed-article:11160680 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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