Please use this identifier to cite or link to this item:
https://biore.bio.bg.ac.rs/handle/123456789/6439
Title: | Protein Disulfide Isomerase Modulates the Activation of Thyroid Hormone Receptors.Front | Authors: | Campos, Jessica L.O. Doratioto, Tabata R. Videira, Natalia B. Ribeiro Filho, Helder V. Batista, Fernanda A. H. Fattori, Juliana Indolfo, Nathalia de C. Nakahira, Marcel Bajgelman, Marcio C. Čvoro, Aleksandra Laurindo, Francisco R. M. Webb, Paul Figueira, Ana Carolina M. |
Keywords: | Nuclear receptor signaling pathways;;Protein complexes;;Protein disulfide isomerase;;Redox regulation;;Thyroid hormone receptor | Issue Date: | Jan-2019 | Rank: | M22 | Journal: | Frontiers in Endocrinology | Volume: | 8 | Issue: | 9 | Start page: | 784 | Abstract: | Thyroid 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. |
URI: | https://biore.bio.bg.ac.rs/handle/123456789/6439 | DOI: | 10.3389/fendo.2018.00784 |
Appears in Collections: | Journal Article |
Show full item record
SCOPUSTM
Citations
3
checked on Nov 4, 2024
Page view(s)
1
checked on Nov 4, 2024
Google ScholarTM
Check
Altmetric
Altmetric
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.