Identificador persistente para citar o vincular este elemento: http://hdl.handle.net/10553/52375
Campo DC Valoridioma
dc.contributor.authorRudd, Michael D.en_US
dc.contributor.authorGonzales-Robayna, Ignacioen_US
dc.contributor.authorHernández, Inmaculadaen_US
dc.contributor.authorWeigel, Nancy L.en_US
dc.contributor.authorBingman, Wiliam E.en_US
dc.contributor.authorRichards, Jo Anne S.en_US
dc.contributor.otherGonzalez Robayna, Ignacio-
dc.contributor.otherHernandez Gonzalez, Inmaculada-
dc.date.accessioned2018-11-25T19:48:16Z-
dc.date.available2018-11-25T19:48:16Z-
dc.date.issued2007en_US
dc.identifier.issn0952-5041en_US
dc.identifier.urihttp://hdl.handle.net/10553/52375-
dc.description.abstractFOXO (Forkhead box O1 transcription factors) factors interact with and modify the activity of other transcription factors, including nuclear hormone receptors. However, not all of the structural domains within the FOXO proteins that mediate these functional interactions have been clearly defined. To address this issue, we used a constitutively active (nuclear) mutant of FOXO1a (designated FOXOA3) and within FOXOA3 made additional mutations to alter the putative nuclear hormone interacting domain (NID), minimal activation domain (MAD), DNA-binding domain (DBD), and the N terminus. We document that FOXOA3 enhanced the hormone-dependent transcriptional activity of liganded progesterone receptors A (PGRA) on a glucocorticoid response element-responsive promoter, PGRA on the insulin-like growth factor-binding protein 1 promoter, and estrogen receptor α on an estrogen response element-responsive promoter. The effects of FOXOA3 on PGRA were dependent, in part, on an intact NID, the MAD, and N-terminal domain. In striking contrast, a FOXOA3 DNA-binding mutant (FOXOA3-mDBD) modulated PGRA, PGRB, and ESR1 activities by distinctly different mechanisms, markedly elevating ligand-independent activity of these nuclear hormone receptors even in the double mutant lacking the MAD. Furthermore, both FOXOA3 and FOXOA3-mDBD enhanced the activity of a transcriptionally defective PGRA lacking its AF1 transactivation domain, indicating that this region of the receptor is not essential in this context. Since FOXOA3, FOXOA3-mDBD, and FOXOA3-mNID all bound PGRA in a GST pull-down assay, it appears that the LXXLL (leucine-X-X-leucine-leucine) motif within the NID is not critical for FOXOA3 interactions with PGRA, but may modify the recruitment of other co-regulatory molecules. Collectively, the results show that FOXOA3 exerts co-regulatory functions independent of DNA binding and that the DNA-binding defective form of FOXO1a is transcriptionally active as a co-regulator of these nuclear hormone receptors.en_US
dc.languageengen_US
dc.relation.ispartofJournal of Molecular Endocrinologyen_US
dc.sourceJournal Of Molecular Endocrinology [ISSN 0952-5041],v. 38 (5-6), p. 673-690 (Mayo-junio 2007)en_US
dc.subject2415 Biología molecularen_US
dc.subject240703 Morfología celularen_US
dc.subject.otherTranscription Factoren_US
dc.subject.otherCell-Cycleen_US
dc.subject.otherNuclear Receptorsen_US
dc.subject.otherLuteinizing-Hormoneen_US
dc.subject.otherGene-Expressionen_US
dc.subject.otherGranulosa-Cellsen_US
dc.subject.otherProteinen_US
dc.subject.otherInsulinen_US
dc.subject.otherActivationen_US
dc.subject.otherFkhren_US
dc.titleConstitutively active FOXO1a and a DNA-binding domain mutant exhibit distinct co-regulatory functions to enhance progesterone receptor A activityen_US
dc.typeinfo:eu-repo/semantics/Articleen_US
dc.typeArticleen_US
dc.identifier.doi10.1677/JME-07-0017en_US
dc.identifier.scopus34347384383-
dc.identifier.isi000247724100013-
dcterms.isPartOfJournal Of Molecular Endocrinology-
dcterms.sourceJournal Of Molecular Endocrinology[ISSN 0952-5041],v. 38 (5-6), p. 673-690-
dc.contributor.authorscopusid8366915100-
dc.contributor.authorscopusid8738000400-
dc.contributor.authorscopusid6507425244-
dc.contributor.authorscopusid16743892400-
dc.contributor.authorscopusid7004999736-
dc.contributor.authorscopusid6506566464-
dc.contributor.authorscopusid56831435300-
dc.contributor.authorscopusid7403707010-
dc.description.lastpage690en_US
dc.identifier.issue5-6-
dc.description.firstpage673en_US
dc.relation.volume38en_US
dc.investigacionCiencias de la Saluden_US
dc.type2Artículoen_US
dc.identifier.wosWOS:000247724100013-
dc.contributor.daisngid264190-
dc.contributor.daisngid2922182-
dc.contributor.daisngid2446020-
dc.contributor.daisngid111703-
dc.contributor.daisngid3390490-
dc.contributor.daisngid63955-
dc.identifier.investigatorRIDK-9671-2014-
dc.identifier.investigatorRIDK-7776-2014-
dc.description.numberofpages18en_US
dc.utils.revisionen_US
dc.contributor.wosstandardWOS:Rudd, MD-
dc.contributor.wosstandardWOS:Gonzalez-Robayna, I-
dc.contributor.wosstandardWOS:Hernandez-Gonzalez, I-
dc.contributor.wosstandardWOS:Weigel, NL-
dc.contributor.wosstandardWOS:Bingman, WE-
dc.contributor.wosstandardWOS:Richards, JS-
dc.date.coverdateMayo-Junio 2007en_US
dc.identifier.ulpgcen_US
dc.contributor.buulpgcBU-MEDen_US
dc.description.jcr2,801-
dc.description.jcrqQ2-
dc.description.scieSCIE-
item.grantfulltextnone-
item.fulltextSin texto completo-
crisitem.author.deptGIR IUIBS: Bioquímica-
crisitem.author.deptIU de Investigaciones Biomédicas y Sanitarias-
crisitem.author.deptDepartamento de Bioquímica y Biología Molecular, Fisiología, Genética e Inmunología-
crisitem.author.deptGIR IUIBS: Bioquímica-
crisitem.author.deptIU de Investigaciones Biomédicas y Sanitarias-
crisitem.author.deptDepartamento de Bioquímica y Biología Molecular, Fisiología, Genética e Inmunología-
crisitem.author.orcid0000-0002-7650-4454-
crisitem.author.orcid0000-0001-8937-9034-
crisitem.author.parentorgIU de Investigaciones Biomédicas y Sanitarias-
crisitem.author.parentorgIU de Investigaciones Biomédicas y Sanitarias-
crisitem.author.fullNameGonzález Robayna, Ignacio Javier-
crisitem.author.fullNameHernández González, Inmaculada Servanda-
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