Please use this identifier to cite or link to this item: https://biore.bio.bg.ac.rs/handle/123456789/6439
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dc.contributor.authorCampos, Jessica L.O.en_US
dc.contributor.authorDoratioto, Tabata R.en_US
dc.contributor.authorVideira, Natalia B.en_US
dc.contributor.authorRibeiro Filho, Helder V.en_US
dc.contributor.authorBatista, Fernanda A. H.en_US
dc.contributor.authorFattori, Julianaen_US
dc.contributor.authorIndolfo, Nathalia de C.en_US
dc.contributor.authorNakahira, Marcelen_US
dc.contributor.authorBajgelman, Marcio C.en_US
dc.contributor.authorČvoro, Aleksandraen_US
dc.contributor.authorLaurindo, Francisco R. M.en_US
dc.contributor.authorWebb, Paulen_US
dc.contributor.authorFigueira, Ana Carolina M.en_US
dc.date.accessioned2023-11-08T11:58:45Z-
dc.date.available2023-11-08T11:58:45Z-
dc.date.issued2019-01-
dc.identifier.urihttps://biore.bio.bg.ac.rs/handle/123456789/6439-
dc.description.abstractThyroid hormone receptors (TRs) are responsible for mediating thyroid hormone (T3 and T4) actions at a cellular level. They belong to the nuclear receptor (NR) superfamily and execute their main functions inside the cell nuclei as hormone-regulated transcription factors. These receptors also exhibit so-called "non-classic" actions, for which other cellular proteins, apart from coregulators inside nuclei, regulate their activity. Aiming to find alternative pathways of TR modulation, we searched for interacting proteins and found that PDIA1 interacts with TRβ in a yeast two-hybrid screening assay. The functional implications of PDIA1-TR interactions are still unclear; however, our co-immunoprecipitation (co-IP) and fluorescence assay results showed that PDI was able to bind both TR isoforms in vitro. Moreover, T3 appears to have no important role in these interactions in cellular assays, where PDIA1 was able to regulate transcription of TRα and TRβ-mediated genes in different ways depending on the promoter region and on the TR isoform involved. Although PDIA1 appears to act as a coregulator, it binds to a TR surface that does not interfere with coactivator binding. However, the TR:PDIA1 complex affinity and activation are different depending on the TR isoform. Such differences may reflect the structural organization of the PDIA1:TR complex, as shown by models depicting an interaction interface with exposed cysteines from both proteins, suggesting that PDIA1 might modulate TR by its thiol reductase/isomerase activity.en_US
dc.language.isoenen_US
dc.relation.ispartofFrontiers in Endocrinologyen_US
dc.subjectNuclear receptor signaling pathways;en_US
dc.subjectProtein complexes;en_US
dc.subjectProtein disulfide isomerase;en_US
dc.subjectRedox regulation;en_US
dc.subjectThyroid hormone receptoren_US
dc.titleProtein Disulfide Isomerase Modulates the Activation of Thyroid Hormone Receptors.Fronten_US
dc.typeArticleen_US
dc.identifier.doi10.3389/fendo.2018.00784-
dc.description.rankM22en_US
dc.description.impact6.055en_US
dc.description.startpage784en_US
dc.relation.issn1664-2392en_US
dc.description.volume8en_US
dc.description.issue9en_US
item.languageiso639-1en-
item.cerifentitytypePublications-
item.openairetypeArticle-
item.fulltextNo Fulltext-
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
crisitem.author.deptChair of Cell and Tissue Biology-
crisitem.author.orcid0009-0007-5643-1634-
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