| pubmed-article:16135792 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C0044602 | lld:lifeskim |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C0033681 | lld:lifeskim |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C0812385 | lld:lifeskim |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C0332466 | lld:lifeskim |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C1418576 | lld:lifeskim |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C1418577 | lld:lifeskim |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C1423080 | lld:lifeskim |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C1423613 | lld:lifeskim |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C0205460 | lld:lifeskim |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:16135792 | lifeskim:mentions | umls-concept:C0686907 | lld:lifeskim |
| pubmed-article:16135792 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:16135792 | pubmed:dateCreated | 2005-9-1 | lld:pubmed |
| pubmed-article:16135792 | pubmed:abstractText | The p85alpha subunit of phosphatidylinositol 3-kinase (PI-3k) forms a complex with a protein network associated with oncogenic fusion tyrosine kinases (FTKs) such as BCR/ABL, TEL/ABL, TEL/JAK2, TEL/PDGFbetaR, and NPM/ALK, resulting in constitutive activation of the p110 catalytic subunit of PI-3k. Introduction of point mutations in the N-terminal and C-terminal SH2 domain and SH3 domain of p85alpha, which disrupt their ability to bind phosphotyrosine and proline-rich motifs, respectively, abrogated their interaction with the BCR/ABL protein network. The p85alpha mutant protein (p85mut) bearing these mutations was unable to interact with BCR/ABL and other FTKs, while its binding to the p110alpha catalytic subunit of PI-3k was intact. In addition, binding of Shc, c-Cbl, and Gab2, but not Crk-L, to p85mut was abrogated. p85mut diminished BCR/ABL-dependent activation of PI-3k and Akt kinase, the downstream effector of PI-3k. This effect was associated with the inhibition of BCR/ABL-dependent growth of the hematopoietic cell line and murine bone marrow cells. Interestingly, the addition of interleukin-3 (IL-3) rescued BCR/ABL-transformed cells from the inhibitory effect of p85mut. SCID mice injected with BCR/ABL-positive hematopoietic cells expressing p85mut survived longer than the animals inoculated with BCR/ABL-transformed counterparts. In conclusion, we have identified the domains of p85alpha responsible for the interaction with the FTK protein network and transduction of leukemogenic signaling. | lld:pubmed |
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| pubmed-article:16135792 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16135792 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16135792 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16135792 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16135792 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16135792 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16135792 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:16135792 | pubmed:author | pubmed-author:SkorskiTomasz... | lld:pubmed |
| pubmed-article:16135792 | pubmed:author | pubmed-author:RenShu-YueSY | lld:pubmed |
| pubmed-article:16135792 | pubmed:author | pubmed-author:NeelBenjamin... | lld:pubmed |
| pubmed-article:16135792 | pubmed:author | pubmed-author:MorrioneAndre... | lld:pubmed |
| pubmed-article:16135792 | pubmed:author | pubmed-author:MohiM GolamMG | lld:pubmed |
| pubmed-article:16135792 | pubmed:author | pubmed-author:BoltonElisabe... | lld:pubmed |
| pubmed-article:16135792 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16135792 | pubmed:volume | 25 | lld:pubmed |
| pubmed-article:16135792 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16135792 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16135792 | pubmed:pagination | 8001-8 | lld:pubmed |
| pubmed-article:16135792 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
