| pubmed-article:14985505 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C0038435 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C0079427 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C2350345 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C0694883 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C1325410 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C1442080 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
| pubmed-article:14985505 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:14985505 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:14985505 | pubmed:dateCreated | 2004-3-10 | lld:pubmed |
| pubmed-article:14985505 | pubmed:abstractText | AMP-activated protein kinase (AMPK) is a highly conserved sensor of cellular energy status found in all eukaryotic cells. AMPK is activated by stimuli that increase the cellular AMP/ATP ratio. Essential to activation of AMPK is its phosphorylation at Thr-172 by an upstream kinase, AMPKK, whose identity in mammalian cells has remained elusive. Here we present biochemical and genetic evidence indicating that the LKB1 serine/threonine kinase, the gene inactivated in the Peutz-Jeghers familial cancer syndrome, is the dominant regulator of AMPK activation in several mammalian cell types. We show that LKB1 directly phosphorylates Thr-172 of AMPKalpha in vitro and activates its kinase activity. LKB1-deficient murine embryonic fibroblasts show nearly complete loss of Thr-172 phosphorylation and downstream AMPK signaling in response to a variety of stimuli that activate AMPK. Reintroduction of WT, but not kinase-dead, LKB1 into these cells restores AMPK activity. Furthermore, we show that LKB1 plays a biologically significant role in this pathway, because LKB1-deficient cells are hypersensitive to apoptosis induced by energy stress. On the basis of these results, we propose a model to explain the apparent paradox that LKB1 is a tumor suppressor, yet cells lacking LKB1 are resistant to cell transformation by conventional oncogenes and are sensitive to killing in response to agents that elevate AMP. The role of LKB1/AMPK in the survival of a subset of genetically defined tumor cells may provide opportunities for cancer therapeutics. | lld:pubmed |
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| pubmed-article:14985505 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14985505 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14985505 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14985505 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14985505 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:14985505 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:14985505 | pubmed:author | pubmed-author:CantleyLewis... | lld:pubmed |
| pubmed-article:14985505 | pubmed:author | pubmed-author:BardeesyNabee... | lld:pubmed |
| pubmed-article:14985505 | pubmed:author | pubmed-author:DePinhoRonald... | lld:pubmed |
| pubmed-article:14985505 | pubmed:author | pubmed-author:HurleyRebecca... | lld:pubmed |
| pubmed-article:14985505 | pubmed:author | pubmed-author:WittersLee... | lld:pubmed |
| pubmed-article:14985505 | pubmed:author | pubmed-author:ShawReuben... | lld:pubmed |
| pubmed-article:14985505 | pubmed:author | pubmed-author:KosmatkaMonic... | lld:pubmed |
| pubmed-article:14985505 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14985505 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:14985505 | pubmed:volume | 101 | lld:pubmed |
| pubmed-article:14985505 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14985505 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14985505 | pubmed:pagination | 3329-35 | lld:pubmed |
| pubmed-article:14985505 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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