| pubmed-article:18480843 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18480843 | lifeskim:mentions | umls-concept:C0006298 | lld:lifeskim |
| pubmed-article:18480843 | lifeskim:mentions | umls-concept:C2350345 | lld:lifeskim |
| pubmed-article:18480843 | lifeskim:mentions | umls-concept:C0013081 | lld:lifeskim |
| pubmed-article:18480843 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:18480843 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:18480843 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:18480843 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:18480843 | pubmed:dateCreated | 2008-6-4 | lld:pubmed |
| pubmed-article:18480843 | pubmed:abstractText | We previously showed that Cidea(-/-) mice are resistant to diet-induced obesity through the upregulation of energy expenditure. The AMP-activated protein kinase (AMPK), consisting of catalytic alpha subunit and regulatory subunits beta and gamma, has a pivotal function in energy homoeostasis. We show here that AMPK protein levels and enzymatic activity were significantly increased in the brown adipose tissue of Cidea(-/-) mice. We also found that Cidea is colocalized with AMPK in the endoplasmic reticulum and forms a complex with AMPK in vivo through specific interaction with the beta subunit of AMPK, but not with the alpha or gamma subunit. When co-expressed with Cidea, the stability of AMPK-beta subunit was dramatically reduced due to increased ubiquitination-mediated degradation, which depends on a physical interaction between Cidea and AMPK. Furthermore, AMPK stability and enzymatic activity were increased in Cidea(-/-) adipocytes differentiated from mouse embryonic fibroblasts or preadipocytes. Our data strongly suggest that AMPK can be regulated by Cidea-mediated ubiquitin-dependent proteosome degradation, and provide a molecular explanation for the increased energy expenditure and lean phenotype in Cidea-null mice. | lld:pubmed |
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| pubmed-article:18480843 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18480843 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18480843 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18480843 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18480843 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18480843 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:18480843 | pubmed:issn | 1460-2075 | lld:pubmed |
| pubmed-article:18480843 | pubmed:author | pubmed-author:LiPengP | lld:pubmed |
| pubmed-article:18480843 | pubmed:author | pubmed-author:ZhouHai-MengH... | lld:pubmed |
| pubmed-article:18480843 | pubmed:author | pubmed-author:ZhaoJieJ | lld:pubmed |
| pubmed-article:18480843 | pubmed:author | pubmed-author:YeJingJ | lld:pubmed |
| pubmed-article:18480843 | pubmed:author | pubmed-author:WuJiaweiJ | lld:pubmed |
| pubmed-article:18480843 | pubmed:author | pubmed-author:LiJohn... | lld:pubmed |
| pubmed-article:18480843 | pubmed:author | pubmed-author:QiJingzongJ | lld:pubmed |
| pubmed-article:18480843 | pubmed:author | pubmed-author:GongJingyiJ | lld:pubmed |
| pubmed-article:18480843 | pubmed:author | pubmed-author:ZhaoTongjinT | lld:pubmed |
| pubmed-article:18480843 | pubmed:author | pubmed-author:LamPennyP | lld:pubmed |
| pubmed-article:18480843 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18480843 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:18480843 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:18480843 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18480843 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18480843 | pubmed:pagination | 1537-48 | lld:pubmed |
| pubmed-article:18480843 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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