| pubmed-article:19927127 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19927127 | lifeskim:mentions | umls-concept:C0231337 | lld:lifeskim |
| pubmed-article:19927127 | lifeskim:mentions | umls-concept:C0032246 | lld:lifeskim |
| pubmed-article:19927127 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:19927127 | lifeskim:mentions | umls-concept:C1826483 | lld:lifeskim |
| pubmed-article:19927127 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:19927127 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:19927127 | pubmed:dateCreated | 2010-1-20 | lld:pubmed |
| pubmed-article:19927127 | pubmed:abstractText | Senescence is an irreversible cell-cycle arrest that is elicited by a wide range of factors, including replicative exhaustion. Emerging evidences suggest that cellular senescence contributes to ageing and acts as a tumour suppressor mechanism. To identify novel genes regulating senescence, we performed a loss-of-function screen on normal human diploid fibroblasts. We show that downregulation of the AMPK-related protein kinase 5 (ARK5 or NUAK1) results in extension of the cellular replicative lifespan. Interestingly, the levels of NUAK1 are upregulated during senescence whereas its ectopic expression triggers a premature senescence. Cells that constitutively express NUAK1 suffer gross aneuploidies and show diminished expression of the genomic stability regulator LATS1, whereas depletion of NUAK1 with shRNA exerts opposite effects. Interestingly, a dominant-negative form of LATS1 phenocopies NUAK1 effects. Moreover, we show that NUAK1 phosphorylates LATS1 at S464 and this has a role in controlling its stability. In summary, our work highlights a novel role for NUAK1 in the control of cellular senescence and cellular ploidy. | lld:pubmed |
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| pubmed-article:19927127 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19927127 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19927127 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19927127 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19927127 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19927127 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19927127 | pubmed:issn | 1460-2075 | lld:pubmed |
| pubmed-article:19927127 | pubmed:author | pubmed-author:de... | lld:pubmed |
| pubmed-article:19927127 | pubmed:author | pubmed-author:CarlingDavidD | lld:pubmed |
| pubmed-article:19927127 | pubmed:author | pubmed-author:WangJingJ | lld:pubmed |
| pubmed-article:19927127 | pubmed:author | pubmed-author:NavaratnamNav... | lld:pubmed |
| pubmed-article:19927127 | pubmed:author | pubmed-author:BernardDavidD | lld:pubmed |
| pubmed-article:19927127 | pubmed:author | pubmed-author:AbbadieCorinn... | lld:pubmed |
| pubmed-article:19927127 | pubmed:author | pubmed-author:HumbertNicola... | lld:pubmed |
| pubmed-article:19927127 | pubmed:author | pubmed-author:MartinezDolor... | lld:pubmed |
| pubmed-article:19927127 | pubmed:author | pubmed-author:GilJesusJ | lld:pubmed |
| pubmed-article:19927127 | pubmed:author | pubmed-author:Da... | lld:pubmed |
| pubmed-article:19927127 | pubmed:author | pubmed-author:MartienSébast... | lld:pubmed |
| pubmed-article:19927127 | pubmed:author | pubmed-author:AugertArnaudA | lld:pubmed |
| pubmed-article:19927127 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19927127 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:19927127 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:19927127 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19927127 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19927127 | pubmed:pagination | 376-86 | lld:pubmed |
| pubmed-article:19927127 | pubmed:dateRevised | 2011-7-20 | lld:pubmed |
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