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dc.contributor.authorMoreno, Daniel-
dc.contributor.authorViana, Rosa-
dc.contributor.authorSanz, Pascual-
dc.date.accessioned2015-03-12T12:49:54Z-
dc.date.available2015-03-12T12:49:54Z-
dc.date.issued2009-12-
dc.identifier.citationInternational Journal of Biochemistry and Cell Biology 41(12):2431-2439. (2009)es_ES
dc.identifier.issn1357-2725-
dc.identifier.urihttp://hdl.handle.net/10261/112294-
dc.description9 páginas, 2 figuras, 5 tablases_ES
dc.description.abstractMammalian 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 AMPK2 (LexA-AMPK2-T172D) co-expressed with AMPK1, LexA-AMPK2 and LexA-AMPK3. 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.es_ES
dc.description.sponsorshipThis work was supported by grants from the Spanish Ministry of Education and Science (SAF2008-01907) and the European Commission (LSHM-CT-2004-005272).es_ES
dc.language.isoenges_ES
dc.publisherBlake and Helsey Editoreses_ES
dc.relation.isversionofPostprintes_ES
dc.rightsopenAccesses_ES
dc.subjectAMPKes_ES
dc.subjectTwo-hybrid screeninges_ES
dc.subjectProteasomees_ES
dc.subjectPSMD11es_ES
dc.subjectPhosphorylationes_ES
dc.titleTwo-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinasees_ES
dc.typeartículoes_ES
dc.identifier.doi10.1016/j.biocel.2009.07.002-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1016/j.biocel.2009.07.002es_ES
dc.identifier.e-issn1878-5875-
dc.relation.csices_ES
dc.identifier.pmid19616115-
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