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dc.contributor.authorRodríguez-Vargas, José Manuel-
dc.contributor.authorRodríguez, María Isabel-
dc.contributor.authorMajuelos-Melguizo, Jara-
dc.contributor.authorGarcía-Diaz, Ángel-
dc.contributor.authorGonzález-Flores, Ariannys-
dc.contributor.authorLópez-Rivas, Abelardo-
dc.contributor.authorDantzer, Françoise-
dc.contributor.authorOliver, Francisco Javier-
dc.date.accessioned2018-05-25T13:08:07Z-
dc.date.available2018-05-25T13:08:07Z-
dc.date.issued2016-
dc.identifierdoi: 10.1038/cdd.2016.80-
dc.identifiere-issn: 1476-5403-
dc.identifierissn: 1350-9047-
dc.identifier.citationCell Death and Differentiation 23(12): 2007-2018 (2016)-
dc.identifier.urihttp://hdl.handle.net/10261/165153-
dc.descriptionRodríguez-Vargas, José Manuel et al.-
dc.description.abstractAMPK is a central energy sensor linking extracellular milieu fluctuations with the autophagic machinery. In the current study we uncover that Poly(ADP-ribosyl)ation (PARylation), a post-translational modification (PTM) of proteins, accounts for the spatial and temporal regulation of autophagy by modulating AMPK subcellular localisation and activation. More particularly, we show that the minority AMPK pool needs to be exported to the cytosol in a PARylation-dependent manner for optimal induction of autophagy, including ULK1 phosphorylation and mTORC1 inactivation. PARP-1 forms a molecular complex with AMPK in the nucleus in non-starved cells. In response to nutrient deprivation, PARP-1 catalysed PARylation, induced the dissociation of the PARP-1/AMPK complex and the export of free PARylated nuclear AMPK to the cytoplasm to activate autophagy. PARP inhibition, its silencing or the expression of PARylation-deficient AMPK mutants prevented not only the AMPK nuclear-cytosolic export but also affected the activation of the cytosolic AMPK pool and autophagosome formation. These results demonstrate that PARylation of AMPK is a key early signal to efficiently convey extracellular nutrient perturbations with downstream events needed for the cell to optimize autophagic commitment before autophagosome formation.-
dc.description.sponsorshipES was supported by Newcastle University's Institute of Neuroscience and MS performed this work as part of her degree in Newcastle University's MRes Programme in Medical and Molecular Biosciences.-
dc.publisherNature Publishing Group-
dc.relation.isversionofPublisher's version-
dc.rightsopenAccess-
dc.titleAutophagy requires poly(adp-ribosyl)ation-dependent AMPK nuclear export-
dc.typeartículo-
dc.identifier.doihttp://dx.doi.org/10.1038/cdd.2016.80-
dc.relation.publisherversionhttps://doi.org/10.1038/cdd.2016.80-
dc.date.updated2018-05-25T13:08:07Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
dc.rights.licensehttp://creativecommons.org/licenses/by-nc-nd/4.0/-
dc.contributor.funderNewcastle University-
dc.relation.csic-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000774es_ES
dc.identifier.pmid27689873-
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