| pubmed-article:18206965 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18206965 | lifeskim:mentions | umls-concept:C1366894 | lld:lifeskim |
| pubmed-article:18206965 | lifeskim:mentions | umls-concept:C0596290 | lld:lifeskim |
| pubmed-article:18206965 | lifeskim:mentions | umls-concept:C0521447 | lld:lifeskim |
| pubmed-article:18206965 | lifeskim:mentions | umls-concept:C0059239 | lld:lifeskim |
| pubmed-article:18206965 | lifeskim:mentions | umls-concept:C0038952 | lld:lifeskim |
| pubmed-article:18206965 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:18206965 | lifeskim:mentions | umls-concept:C0079419 | lld:lifeskim |
| pubmed-article:18206965 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:18206965 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:18206965 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:18206965 | pubmed:dateCreated | 2008-1-21 | lld:pubmed |
| pubmed-article:18206965 | pubmed:abstractText | FAK is known as an integrin- and growth factor-associated tyrosine kinase promoting cell motility. Here we show that, during mouse development, FAK inactivation results in p53- and p21-dependent mesodermal cell growth arrest. Reconstitution of primary FAK-/-p21-/- fibroblasts revealed that FAK, in a kinase-independent manner, facilitates p53 turnover via enhanced Mdm2-dependent p53 ubiquitination. p53 inactivation by FAK required FAK FERM F1 lobe binding to p53, FERM F2 lobe-mediated nuclear localization, and FERM F3 lobe for connections to Mdm2 and proteasomal degradation. Staurosporine or loss of cell adhesion enhanced FERM-dependent FAK nuclear accumulation. In primary human cells, FAK knockdown raised p53-p21 levels and slowed cell proliferation but did not cause apoptosis. Notably, FAK knockdown plus cisplatin triggered p53-dependent cell apoptosis, which was rescued by either full-length FAK or FAK FERM re-expression. These studies define a scaffolding role for nuclear FAK in facilitating cell survival through enhanced p53 degradation under conditions of cellular stress. | lld:pubmed |
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| pubmed-article:18206965 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18206965 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18206965 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18206965 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18206965 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:18206965 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:18206965 | pubmed:author | pubmed-author:LimYangmiY | lld:pubmed |
| pubmed-article:18206965 | pubmed:author | pubmed-author:FisherSusan... | lld:pubmed |
| pubmed-article:18206965 | pubmed:author | pubmed-author:SchlaepferDav... | lld:pubmed |
| pubmed-article:18206965 | pubmed:author | pubmed-author:IlicDuskoD | lld:pubmed |
| pubmed-article:18206965 | pubmed:author | pubmed-author:LimSsang-Taek... | lld:pubmed |
| pubmed-article:18206965 | pubmed:author | pubmed-author:HowertonKyleK | lld:pubmed |
| pubmed-article:18206965 | pubmed:author | pubmed-author:VoThanh-Trang... | lld:pubmed |
| pubmed-article:18206965 | pubmed:author | pubmed-author:HansonDan ADA | lld:pubmed |
| pubmed-article:18206965 | pubmed:author | pubmed-author:LarocqueNicho... | lld:pubmed |
| pubmed-article:18206965 | pubmed:author | pubmed-author:ChenXiao... | lld:pubmed |
| pubmed-article:18206965 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18206965 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:18206965 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:18206965 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18206965 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18206965 | pubmed:pagination | 9-22 | lld:pubmed |
| pubmed-article:18206965 | pubmed:dateRevised | 2011-3-9 | lld:pubmed |
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