ArticleEuropean thyroid journal2016
Impaired Repressor Function in SUMOylation-Defective Thyroid Hormone Receptor Isoforms.
Article in European thyroid journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 7 citations in OpenAlex.
- Acetylation modulates thyroid hormone receptor intracellular localization and intranuclear mobility.Molecular and cellular endocrinology · 2019Article
- Thyroid hormone receptor localization in target tissues.The Journal of endocrinology · 2018Review
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMany nuclear receptors are modified by posttranslational modifications.
objectivesThe transcriptional activity of thyroid hormone receptors (TRs) is modified by the influence of its ligand (thyroid hormones T
methodsSUMOylation of TR wild-type as well as isoform-specific point mutations have been studied in vitro. The promoter occupancy of TR (wild-type and double- or triple-mutated versions) and transcriptional cofactors have been investigated in chromatin immunoprecipitation (ChIP) and Re-ChIP analysis.
resultsTR is modified by SUMO proteins at defined residues: the isoform TRα is mainly modified at lysines 281 and 387, whereas lysines 50 and 443 are major SUMOylation sites of isoform TRβ. Lysine residues K281 (TRα) and K50 (TRβ) are isoform-specific SUMOylation sites influencing differing TR domains, whereas K387 (TRα) and K443 (TRβ) are orthologous residues. TRs are targets of all three SUMO variants (SUMO-1, -2, and -3). The transcriptional activity of SUMOylation-defective mutants of TR alters gene transcription from positively and negatively regulated T
conclusionsThe most pronounced effect is an impaired repressor function of SUMOylation-deficient TR in the absence of T
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