ArticleMolecular and cellular biology1993
A conserved C-terminal sequence that is deleted in v-ErbA is essential for the biological activities of c-ErbA (the thyroid hormone receptor).
Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 101 citations in OpenAlex.
- Nuclear receptor coregulator interactions: beyond the switch.Genes & development · 2026Review
- Thyroid Hormone Signaling Pathways: Time for a More Precise Nomenclature.Endocrinology · 2017Article
- Article
- Factor recruitment and TIF2/GRIP1 corepressor activity at a collagenase-3 response element that mediates regulation by phorbol esters and hormones.The EMBO journal · 2001Article
- Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-erbA yields a chromatin infrastructure-dependent transcriptional repression pathway.The EMBO journal · 2000Article
- Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors.Molecular and cellular biology · 2000Article
- Leukemic transformation by the v-ErbA oncoprotein entails constitutive binding to and repression of an erythroid enhancer in vivo.The EMBO journal · 1998Article
- The thyroid hormone receptor functions as a ligand-operated developmental switch between proliferation and differentiation of erythroid progenitors.The EMBO journal · 1998Article
- Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor.The EMBO journal · 1998Article
- Nuclear hormone receptor antagonism with AP-1 by inhibition of the JNK pathway.Genes & development · 1997Article
- Expression of the thyroid hormone receptor gene, erbAalpha, in B lymphocytes: alternative mRNA processing is independent of differentiation but correlates with antisense RNA levels.Nucleic acids research · 1997Article
- A conformational switch in nuclear hormone receptors is involved in coupling hormone binding to corepressor release.Molecular and cellular biology · 1997Article
- A mutation mimicking ligand-induced conformational change yields a constitutive RXR that senses allosteric effects in heterodimers.The EMBO journal · 1997Article
- Functional domains of the human orphan receptor ARP-1/COUP-TFII involved in active repression and transrepression.Molecular and cellular biology · 1997Article
- Mutations in the conserved C-terminal sequence in thyroid hormone receptor dissociate hormone-dependent activation from interference with AP-1 activity.Molecular and cellular biology · 1997Article
- Nuclear receptor corepressors activate rather than suppress basal transcription of genes that are negatively regulated by thyroid hormone.Molecular and cellular biology · 1997Article
- AF-2 activity and recruitment of steroid receptor coactivator 1 to the estrogen receptor depend on a lysine residue conserved in nuclear receptors.Molecular and cellular biology · 1997Article
- Ligand-independent activation of the oestrogen receptor by mutation of a conserved tyrosine.The EMBO journal · 1997Article
- A natural transactivation mutation in the thyroid hormone beta receptor: impaired interaction with putative transcriptional mediators.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- RIP-140 interacts with multiple nuclear receptors by means of two distinct sites.Molecular and cellular biology · 1996Article
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5 authors at 2 institutions in 2 countries.
Funding
Abstract
The thyroid hormone (T3) receptor type alpha, the c-ErbA alpha proto-oncoprotein, stimulates transcription of T3-dependent promoters, interferes with AP-1 activity, and induces erythroid differentiation in a ligand-dependent manner. The v-ErbA oncoprotein does not bind hormone and has lost all of these activities. Using c-ErbA/v-ErbA chimeras, we found that a deletion of 9 amino acids, conserved among many members of the nuclear receptor superfamily, which are located at the extreme carboxy terminus of c-ErbA alpha is responsible for loss of both transactivation and transcriptional interference activities. Single, double, and triple amino acid substitutions within this region completely abolished T3-dependent transcriptional activation, interference with AP-1 activity, and decreased T3 binding by c-ErbA alpha. However, the lower T3 binding by these mutants does not fully account for the loss of transactivation and transcriptional interference, since a c-ErbA/v-ErbA chimera which was similarly reduced in T3 binding activity has retained both of these functions. Deletion of homologous residues in the retinoic acid receptor alpha (RAR alpha) resulted in a similar loss of transactivation and transcriptional interference activities. The ability of c-ErbA alpha to induce differentiation of transformed erythroblasts is also impaired by all of the mutations introduced into the conserved carboxy-terminal sequence. We conclude that this 9-amino-acid conserved region is essential for normal biological function of c-ErbA alpha and RAR alpha and possibly other T3 and RA receptors.
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