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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Protein Disulfide Isomerase Modulates the Activation of Thyroid Hormone Receptors

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Author(s):
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Campos, Jessica L. O. [1, 2] ; Doratioto, Tabata R. [1, 2] ; Videira, Natalia B. [1, 2] ; Ribeiro Filho, V, Helder ; Batista, Fernanda A. H. [3] ; Fattori, Juliana [3] ; Indolfo, Nathalia de C. [3, 4] ; Nakahira, Marcel [5] ; Bajgelman, Marcio C. [3] ; Cvoro, Aleksandra [6] ; Laurindo, Francisco R. M. [7] ; Webb, Paul [8] ; Figueira, Ana Carolina M. [3]
Total Authors: 13
Affiliation:
[1] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Biosci Natl Lab LNBio, Sao Paulo - Brazil
[2] State Univ Campinas Unicamp, Inst Biol, Grad Program Biosci & Bioact Prod Technol, Sao Paulo - Brazil
[3] Ribeiro Filho, Helder, V, Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Biosci Natl Lab LNBio, Sao Paulo - Brazil
[4] Ribeiro Filho, Helder, V, State Univ Campinas Unicamp, Inst Biol, Grad Program Biosci & Bioact Prod Technol, Sao Paulo - Brazil
[5] State Univ Campinas Unicamp, Inst Chem IQ, Sao Paulo - Brazil
[6] Methodist Hosp Res Inst, Genom Med, Houston, TX - USA
[7] Univ Sao Paulo, Sch Med, Vasc Biol Lab, Heart Inst InCor, Sao Paulo - Brazil
[8] Calif Inst Regenerat Med, Oakland, CA - USA
Total Affiliations: 8
Document type: Journal article
Source: FRONTIERS IN ENDOCRINOLOGY; v. 9, JAN 8 2019.
Web of Science Citations: 0
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 TR beta) 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 TR alpha and TR beta-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. (AU)

FAPESP's process: 16/22246-0 - PPAR gamma repression mechanism as a target to combat diabetes and obesity
Grantee:Ana Carolina Migliorini Figueira
Support type: Regular Research Grants
FAPESP's process: 13/07937-8 - Redoxome - Redox Processes in Biomedicine
Grantee:Ohara Augusto
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 11/23659-2 - Interaction between nuclear receptors TR (thyroid hormone receptor), PPAR (Peroxissome Proliferator-Activated Receptor) and other cell proteins
Grantee:Jéssica Christina Lóis de Oliveira Campos
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 14/22215-1 - New signaling pathways modulated by thyroid hormone receptor (TR) in breast cancer
Grantee:Jéssica Christina Lóis de Oliveira Campos
Support type: Scholarships abroad - Research Internship - Doctorate (Direct)
FAPESP's process: 13/08743-2 - Identification and characterization of new interactions among thyroid hormone receptors and proteins
Grantee:Ana Carolina Migliorini Figueira
Support type: Regular Research Grants