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dc.creatorRivero Rodríguez, Franciscoes
dc.creatorDíaz Quintana, Antonio Jesúses
dc.creatorVelázquez Cruz, Alejandroes
dc.creatorGonzález Arzola, Katiuskaes
dc.creatorGavilán Dorronzoro, María de la Pazes
dc.creatorVelázquez Campoy, Adriánes
dc.creatorRíos Sánchez, Rosa Maríaes
dc.creatorRosa Acosta, Miguel Ángel de laes
dc.creatorDíaz Moreno, Irenees
dc.date.accessioned2021-08-30T11:51:50Z
dc.date.available2021-08-30T11:51:50Z
dc.date.issued2021
dc.identifier.citationRivero Rodríguez, F., Díaz Quintana, A.J., Velázquez Cruz, A., González Arzola, K., Gavilán Dorronzoro, M.d.l.P., Velázquez Campoy, A.,...,Díaz Moreno, I. (2021). Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c. Redox Biology, 43, 101967.
dc.identifier.issn2213-2317es
dc.identifier.urihttps://hdl.handle.net/11441/125217
dc.description.abstractRepair of injured DNA relies on nucleosome dismantling by histone chaperones and de-phosphorylation events carried out by Protein Phosphatase 2A (PP2A). Typical histone chaperones are the Acidic leucine-rich Nuclear Phosphoprotein 32 family (ANP32) members, e.g. ANP32A, which is also a well-known PP2A inhibitor (a.k.a. I1PP2A). Here we report the novel interaction between the endogenous family member B—so-called ANP32B—and endogenous cytochrome c in cells undergoing camptothecin-induced DNA damage. Soon after DNA lesions but prior to caspase cascade activation, the hemeprotein translocates to the nucleus to target the Low Complexity Acidic Region (LCAR) of ANP32B; in a similar way, our group recently reported that the hemeprotein targets the acidic domain of SET/Template Activating Factor-Iβ (SET/TAF-Iβ), which is another histone chaperone and PP2A inhibitor (a.k.a. I2PP2A). The nucleosome assembly activity of ANP32B is indeed unaffected by cytochrome c binding. Like ANP32A, ANP32B inhibits PP2A activity and is thus herein referred to as I3PP2A. Our data demonstrates that ANP32B-dependent inhibition of PP2A is regulated by respiratory cytochrome c, which induces long-distance allosteric changes in the structured N-terminal domain of ANP32B upon binding to the C-terminal LCAR. In agreement with the reported role of PP2A in the DNA damage response, we propose a model wherein cytochrome c is translocated from the mitochondria into the nucleus upon DNA damage to modulate PP2A activity via its interaction with ANP32B.es
dc.formatapplication/pdfes
dc.format.extent17 p.es
dc.language.isoenges
dc.publisherElsevieres
dc.relation.ispartofRedox Biology, 43, 101967.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectHistone chaperonees
dc.subjectNuclear magnetic resonancees
dc.subjectMolecular dynamicses
dc.subjectProtein-protein interactionses
dc.subjectCytochrome ces
dc.titleInhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome ces
dc.typeinfo:eu-repo/semantics/articlees
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessrightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Moleculares
dc.relation.publisherversionhttp://dx.doi.org/10.1016/j.redox.2021.101967es
dc.identifier.doi10.1016/j.redox.2021.101967es
dc.journaltitleRedox Biologyes
dc.publication.volumen43es
dc.publication.endPage101967es

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