| pubmed-article:10430888 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10430888 | lifeskim:mentions | umls-concept:C0031671 | lld:lifeskim |
| pubmed-article:10430888 | lifeskim:mentions | umls-concept:C0059239 | lld:lifeskim |
| pubmed-article:10430888 | lifeskim:mentions | umls-concept:C1565434 | lld:lifeskim |
| pubmed-article:10430888 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:10430888 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:10430888 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:10430888 | pubmed:dateCreated | 1999-9-9 | lld:pubmed |
| pubmed-article:10430888 | pubmed:abstractText | The nonreceptor tyrosine kinase FAK ("focal adhesion kinase") is a key mediator of integrin signaling events controlling cellular responses to the extracellular matrix, including spreading, migration, proliferation, and survival. Integrin-ligand interactions stimulate FAK tyrosine phosphorylation and activation of FAK signaling functions. Here evidence is presented that the FAK autophosphorylation site Tyr-397 mediates a direct interaction with the C-terminal Src homology 2 domain of phospholipase C (PLC)-gamma1 and that this is required for both adhesion-dependent association of the two molecules and increased inositol phosphate production in mouse embryo fibroblasts. Overexpression of FAK and PLC-gamma1 in COS-7 cells increases PLC-gamma1 enzymatic activity and tyrosine phosphorylation, also dependent on FAK Tyr-397. However, FAK appears incapable of directly phosphorylating PLC-gamma1. These observations suggest a role for FAK in recruiting PLC-gamma1 to the plasma membrane at sites of cell-matrix adhesion and there promoting its enzymatic activity, possibly by releasing the repression caused by intramolecular interactions of the PLC-gamma1 Src homology domains and/or by positioning it for phosphorylation by associated Src-family kinases. These findings expand the known signaling functions of FAK and provide mechanistic insight into integrin-stimulation of PLC-gamma1. | lld:pubmed |
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| pubmed-article:10430888 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10430888 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10430888 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10430888 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10430888 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10430888 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:10430888 | pubmed:author | pubmed-author:CarpenterGG | lld:pubmed |
| pubmed-article:10430888 | pubmed:author | pubmed-author:OwenJ DJD | lld:pubmed |
| pubmed-article:10430888 | pubmed:author | pubmed-author:Chattopadhyay... | lld:pubmed |
| pubmed-article:10430888 | pubmed:author | pubmed-author:ZhangXX | lld:pubmed |
| pubmed-article:10430888 | pubmed:author | pubmed-author:HanksS KSK | lld:pubmed |
| pubmed-article:10430888 | pubmed:author | pubmed-author:JiQ SQS | lld:pubmed |
| pubmed-article:10430888 | pubmed:author | pubmed-author:RuestP JPJ | lld:pubmed |
| pubmed-article:10430888 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10430888 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:10430888 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:10430888 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10430888 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10430888 | pubmed:pagination | 9021-6 | lld:pubmed |
| pubmed-article:10430888 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:10430888 | pubmed:meshHeading | pubmed-meshheading:10430888... | lld:pubmed |
| pubmed-article:10430888 | pubmed:meshHeading | pubmed-meshheading:10430888... | lld:pubmed |
| pubmed-article:10430888 | pubmed:meshHeading | pubmed-meshheading:10430888... | lld:pubmed |
| pubmed-article:10430888 | pubmed:meshHeading | pubmed-meshheading:10430888... | lld:pubmed |
