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Article

Lack of coactivator interaction can be a mechanism for dominant negative activity by mutant thyroid hormone receptors.

Endocrinology - 1 Oct 1998

Liu Y, Takeshita A, Misiti S, Chin W W, Yen P M

Abstract excerpt

We studied the interactions of two natural thyroid hormone receptor (TR) mutants from patients with resistance to thyroid hormone (RTH) and an artificial TR mutant with a nuclear receptor corepressor, N-CoR, and a steroid receptor coactivator, SRC-1. In electrophoretic mobility shift assays, wild-type TRbeta-1 interacted with N-CoR in the absence of ligand, whereas T3 caused dissociation of the TRbeta-1/N-CoR...

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Source

Identifiers

PMID: 9751500
DOI: 10.1210/endo.139.10.6218

Genes

SRC

Variants

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Lack of coactivator interaction can be a mechanism for dominant negative activity by mutant thyroid hormone receptors.PMID 9751500Read ↗

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A novel natural mutation in the thyroid hormone receptor defines a dual functional domain that exchanges nuclear receptor corepressors and coactivators.Semantic proximity Read ↗

Nuclear corepressors enhance the dominant negative activity of mutant receptors that cause resistance to thyroid hormone.Semantic proximity Read ↗

Thyroid hormone resistance syndrome manifests as an aberrant interaction between mutant T3 receptors and transcriptional corepressors.Semantic proximity Read ↗

Thyroid hormone signaling in vivo requires a balance between coactivators and corepressors.Semantic proximity Read ↗

Resistance to thyroid hormone (RTH) syndrome reveals novel determinants regulating interaction of T3 receptor with corepressor.Semantic proximity Read ↗

N-terminal variants of thyroid hormone receptor beta: differential function and potential contribution to syndrome of resistance to thyroid hormone.Semantic proximity Read ↗

Thyroid hormone resistance syndrome. Inhibition of normal receptor function by mutant thyroid hormone receptors.Semantic proximity Read ↗

A role for helix 3 of the TRbeta ligand-binding domain in coactivator recruitment identified by characterization of a third cluster of mutations in resistance to thyroid hormone.Semantic proximity Read ↗

Resistance to thyroid hormone is modulated in vivo by the nuclear receptor corepressor (NCOR1).Semantic proximity Read ↗

A Novel TRβ Mutation (R383H) in Resistance to Thyroid Hormone Syndrome Predominantly Impairs Corepressor Release and Negative Transcriptional RegulationSemantic proximity Read ↗

Very strong correlation between dominant negative activities of mutant thyroid hormone receptors and their binding avidity for corepressor SMRT.Semantic proximity Read ↗

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