ArticleMolecular and cellular biology1993
The erbA oncogene represses the actions of both retinoid X and retinoid A receptors but does so by distinct mechanisms.
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 21 papers.
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Who cites it
21 citing papers in PubMed, 51 citations in OpenAlex.
- Analysis of Thyroid Tumorigenesis in Xenograft Mouse Model.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Thyroid hormone receptors and cancer.Biochimica et biophysica acta · 2013Review
- Modeling follicular thyroid cancer for future therapies.American journal of cancer research · 2012Article
- DNA recognition by thyroid hormone and retinoic acid receptors: 3,4,5 rule modified.Molecular and cellular endocrinology · 2010Article
- Thyroid hormone receptors are tumor suppressors in a mouse model of metastatic follicular thyroid carcinoma.Oncogene · 2010Article
- Response of SMRT (silencing mediator of retinoic acid and thyroid hormone receptor) and N-CoR (nuclear receptor corepressor) corepressors to mitogen-activated protein kinase kinase kinase cascades is determined by alternative mRNA splicing.Molecular endocrinology (Baltimore, Md.) · 2007Article
- Article
- Heterodimers of retinoic acid receptors and thyroid hormone receptors display unique combinatorial regulatory properties.Molecular endocrinology (Baltimore, Md.) · 2005Article
- Alternative mRNA splicing of SMRT creates functional diversity by generating corepressor isoforms with different affinities for different nuclear receptors.The Journal of biological chemistry · 2005Article
- SMRT and N-CoR corepressors are regulated by distinct kinase signaling pathways.The Journal of biological chemistry · 2004Article
- Retinoid isomers differ in the ability to induce release of SMRT corepressor from retinoic acid receptor-alpha.The Journal of biological chemistry · 1999Article
- Transcriptional silencing is defined by isoform- and heterodimer-specific interactions between nuclear hormone receptors and corepressors.Molecular and cellular biology · 1998Article
- Transcriptional repression by the SMRT-mSin3 corepressor: multiple interactions, multiple mechanisms, and a potential role for TFIIB.Molecular and cellular biology · 1998Article
- Differential recognition of liganded and unliganded thyroid hormone receptor by retinoid X receptor regulates transcriptional repression.Molecular and cellular biology · 1997Article
- A conformational switch in nuclear hormone receptors is involved in coupling hormone binding to corepressor release.Molecular and cellular biology · 1997Article
- Myb-Ets fusion oncoprotein inhibits thyroid hormone receptor/c-ErbA and retinoic acid receptor functions: a novel mechanism of action for leukemogenic transformation by E26 avian retrovirus.Molecular and cellular biology · 1996Article
- The transcriptional transactivator of simian foamy virus 1 binds to a DNA target element in the viral internal promoter.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Tissue-specific distribution of a novel C-terminal truncation retinoic acid receptor mutant which acts as a negative repressor in a promoter- and cell-type-specific manner.Molecular and cellular biology · 1995Article
- Cooperative formation of high-order oligomers by retinoid X receptors: an unexpected mode of DNA recognition.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Retinoid X receptor alpha transactivates the hepatitis B virus enhancer 1 element by forming a heterodimeric complex with the peroxisome proliferator-activated receptor.Journal of virology · 1995Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Genetic lesions that function as dominant negative mutations in microbial systems have long been recognized. It is only relatively recently, however, that similar dominant negative mutations have been implicated as a basis for genetic and neoplastic disorders in vertebrates. We describe here a dissection of the actions of the erbA oncogene protein, an aberrant form of thyroid hormone receptor that acts as a dominant negative inhibitor of other nuclear hormone receptors. We demonstrate that the ErbA oncoprotein interferes with thyroid hormone and trans-retinoic acid receptors by competing for binding to the corresponding response elements. Heterodimerization of the ErbA oncoprotein with these receptors does not play an observable role in repression. In contrast, however, the ErbA oncoprotein does efficiently form a heterodimer with the retinoid X receptor (RXR) class of nuclear hormone receptors; complex formation enhances the DNA-binding properties of the ErbA protein but dramatically interferes with the ability of the RXR component to activate gene expression. Our results indicate that the erbA oncogene may play a previously unanticipated role in neoplasia by interfering with RXR function.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.