| pubmed-article:12697812 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12697812 | lifeskim:mentions | umls-concept:C0080298 | lld:lifeskim |
| pubmed-article:12697812 | lifeskim:mentions | umls-concept:C0596290 | lld:lifeskim |
| pubmed-article:12697812 | lifeskim:mentions | umls-concept:C0031670 | lld:lifeskim |
| pubmed-article:12697812 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:12697812 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:12697812 | pubmed:dateCreated | 2003-4-16 | lld:pubmed |
| pubmed-article:12697812 | pubmed:abstractText | Phospholipase D (PLD) has been implicated in the signal transduction pathways initiated by several mitogenic protein tyrosine kinases. We demonstrate for the first time that most notably PLD2 and to a lesser extent the PLD1 isoform are tyrosine phosphorylated by c-Src tyrosine kinase via direct association. Moreover, epidermal growth factor induced tyrosine phosphorylation of PLD2 and its interaction with c-Src in A431 cells. Interaction between these proteins is via the pleckstrin homology domain of PLD2 and the catalytic domain of c-Src. Coexpression of PLD1 or PLD2 with c-Src synergistically enhances cellular proliferation compared with expression of either molecule. While PLD activity as a lipid-hydrolyzing enzyme is not affected by c-Src, wild-type PLDs but not catalytically inactive PLD mutants significantly increase c-Src kinase activity, up-regulating c-Src-mediated paxillin phosphorylation and extracellular signal-regulated kinase activity. These results demonstrate the critical role of PLD catalytic activity in the stimulation of Src signaling. In conclusion, we provide the first evidence that c-Src acts as a kinase of PLD and PLD acts as an activator of c-Src. This transmodulation between c-Src and PLD may contribute to the promotion of cellular proliferation via amplification of mitogenic signaling pathways. | lld:pubmed |
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| pubmed-article:12697812 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12697812 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12697812 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12697812 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12697812 | pubmed:month | May | lld:pubmed |
| pubmed-article:12697812 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:12697812 | pubmed:author | pubmed-author:LeeYoung... | lld:pubmed |
| pubmed-article:12697812 | pubmed:author | pubmed-author:MinDo SikDS | lld:pubmed |
| pubmed-article:12697812 | pubmed:author | pubmed-author:JoYang-HyeokY... | lld:pubmed |
| pubmed-article:12697812 | pubmed:author | pubmed-author:KwonTaeg... | lld:pubmed |
| pubmed-article:12697812 | pubmed:author | pubmed-author:KimMyung-SukM... | lld:pubmed |
| pubmed-article:12697812 | pubmed:author | pubmed-author:AhnBong-HyunB... | lld:pubmed |
| pubmed-article:12697812 | pubmed:author | pubmed-author:KimShi YeonSY | lld:pubmed |
| pubmed-article:12697812 | pubmed:author | pubmed-author:ChangJong-Soo... | lld:pubmed |
| pubmed-article:12697812 | pubmed:author | pubmed-author:ChoiKyeong... | lld:pubmed |
| pubmed-article:12697812 | pubmed:author | pubmed-author:KimEun HeeEH | lld:pubmed |
| pubmed-article:12697812 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12697812 | pubmed:volume | 23 | lld:pubmed |
| pubmed-article:12697812 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12697812 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12697812 | pubmed:pagination | 3103-15 | lld:pubmed |
| pubmed-article:12697812 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
| pubmed-article:12697812 | pubmed:meshHeading | pubmed-meshheading:12697812... | lld:pubmed |
