| pubmed-article:19616115 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19616115 | lifeskim:mentions | umls-concept:C0682323 | lld:lifeskim |
| pubmed-article:19616115 | lifeskim:mentions | umls-concept:C0208355 | lld:lifeskim |
| pubmed-article:19616115 | lifeskim:mentions | umls-concept:C2350345 | lld:lifeskim |
| pubmed-article:19616115 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:19616115 | lifeskim:mentions | umls-concept:C1419029 | lld:lifeskim |
| pubmed-article:19616115 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:19616115 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:19616115 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:19616115 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:19616115 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:19616115 | pubmed:dateCreated | 2009-11-2 | lld:pubmed |
| pubmed-article:19616115 | pubmed:abstractText | Mammalian AMP-activated protein kinase (AMPK) is a heterotrimeric serine/threonine protein kinase that acts as a sensor of cellular energy status. It interacts with a great variety of different substrates leading to short-term (i.e. regulation of the activity of different enzymes by direct phosphorylation) and long-term effects (i.e. regulation of transcriptional activity of different transcription factors). In this work, we describe the use of the yeast two-hybrid technology to identify additional proteins that interact with the different subunits of AMPK. We have performed three yeast two-hybrid screenings of a human skeletal muscle cDNA library using three different baits: a constitutively active form of AMPKalpha2 (LexA-AMPKalpha2-T172D) co-expressed with AMPKgamma1, LexA-AMPKbeta2 and LexA-AMPKgamma3. Our results identify novel interaction partners of AMPK in human skeletal muscle. We also further characterize the interaction of AMPK with one of these novel interacting proteins, the non-ATPase subunit of the proteasome PSMD11. Our results indicate that AMPK is able to interact physically with this subunit and modify its phosphorylation status, supporting a possible role for AMPK in regulating proteasome function. | lld:pubmed |
| pubmed-article:19616115 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19616115 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19616115 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19616115 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19616115 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:19616115 | pubmed:issn | 1878-5875 | lld:pubmed |
| pubmed-article:19616115 | pubmed:author | pubmed-author:SanzPascualP | lld:pubmed |
| pubmed-article:19616115 | pubmed:author | pubmed-author:VianaRosaR | lld:pubmed |
| pubmed-article:19616115 | pubmed:author | pubmed-author:MorenoDanielD | lld:pubmed |
| pubmed-article:19616115 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19616115 | pubmed:volume | 41 | lld:pubmed |
| pubmed-article:19616115 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19616115 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19616115 | pubmed:pagination | 2431-9 | lld:pubmed |
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| pubmed-article:19616115 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19616115 | pubmed:articleTitle | Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase. | lld:pubmed |
| pubmed-article:19616115 | pubmed:affiliation | Instituto de Biomedicina de Valencia, CSIC and CIBER de Enfermedades Raras (CIBERER), Jaime Roig 11, 46010 Valencia, Spain. | lld:pubmed |
| pubmed-article:19616115 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19616115 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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