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Regulation of NFAT by poly(ADP-ribose) polymerase activity in T cells

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dc.contributor.authorSchreiber, Valerie
dc.contributor.authorSaenz, Luis
dc.contributor.authorMartínez, Teresa
dc.contributor.authorMunoz Suano, Alba
dc.contributor.authorDominguez Villar, Margarita
dc.contributor.authorRamírez, Pablo
dc.contributor.authorParrilla, Pascual
dc.contributor.authorAguado, Enrique
dc.contributor.authorGarcía Cózar, Francisco
dc.contributor.authorYélamos, José
dc.contributor.authorValdor Alonso, Rut
dc.contributor.departmentBioquímica y Biología Molecular B e Inmunología
dc.date.accessioned2024-02-07T11:57:42Z
dc.date.available2024-02-07T11:57:42Z
dc.date.issued2007-10-31
dc.description©2007. This document is the published, version of a Published Work that appeared in final form in Molecular Immunology. To access the final edited and published work see https://doi.org/10.1016/j.molimm.2007.10.044
dc.description.abstractThe nuclear factor of activated T cells (NFAT) family of transcription factors is pivotal for T lymphocyte functionality. All relevant NFAT activation events upon T cells stimulation such as nuclear translocation, DNA binding, and transcriptional activity have been shown to be dictated by its phosphorylation state. Here, we provide evidence for a novel post- translational modification that regulates NFAT. Indeed, NFATc1 and NFATc2 are poly(ADP-ribosyl)ated by poly-ADP-ribose polymerase-1 (PARP-1). Moreover, we have also found a physical interaction between PARP-1 and both NFATc1 and NFATc2. Interestingly, PARP is activated during T cell stimulation in the absence of DNA damage, leading to ADP-ribose polymers formation and transfer to nuclear acceptor proteins. Our data suggest that poly(ADP-ribosyl)ation modulates the activation of NFAT in T cells, as PARP inhibition causes an increase in NFAT-dependent transactivation and a delay in NFAT nuclear export. Poly(ADPribosyl)ation will expedited NFAT export from the nucleus directly or by priming/facilitating NFAT phosphorylation. Altogether, these data point to PARP-1 and poly(ADP-ribosyl)ation as a novel regulatory mechanism of NFAT at nuclear level, suggesting a potential use of PARP as a new therapeutic target in the modulation of NFAT.
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dc.format.extent9
dc.identifier.citationMolecular Immunology 45 (2008) 1863–1871
dc.identifier.doihttps://doi.org/10.1016/j.molimm.2007.10.044
dc.identifier.issnPrint: 0161-5890
dc.identifier.urihttp://hdl.handle.net/10201/138879
dc.languageenges
dc.publisherElsevier
dc.relationThis work was supported by The Spanish Ministerio de Educacion y Ciencia (grants BIO-2005- ´ 01393, SAF2005-00458, Programa Ramon y Cajal to FJGC), ´ Instituto de Salud Carlos III (grant CP06/00021), Fundacion´ Seneca (grants 00603/PI/0403055/PI/05) and funds from The ´Centre National de la Recherche Scientifique, Association pour la Recherche contre le Cancer, Electricite de France, Comit ´ e du ´ Haut-Rhin de la Ligue Nationale Contre le Cancer and Commissariat a l’Energie Atomique. RV, MDV, and AMS are graduate ` fellows from Fundacion S ´ eneca, Instituto de Salud Carlos III ´ and Junta de Andalucia, respectively.es
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectNFAT
dc.subjectNuclear retention
dc.subjectPoly-ADP ribose polymerases
dc.subjectPoly(ADP-ribosyl)ation
dc.titleRegulation of NFAT by poly(ADP-ribose) polymerase activity in T cellses
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
relation.isAuthorOfPublication3c8bdde5-45b4-462a-976d-8a05dd6d2f5d
relation.isAuthorOfPublication.latestForDiscovery3c8bdde5-45b4-462a-976d-8a05dd6d2f5d
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