Requirement for the C-terminal domain of the v-erbA oncogene protein for biological function and transcriptional repression.

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Article

Requirement for the C-terminal domain of the v-erbA oncogene protein for biological function and transcriptional repression.

Oncogene - 1 Mar 1990

Forrest D, Muñoz A, Raynoschek C, Vennström B, Beug H

Abstract excerpt

In contrast to the normal thyroid hormone receptor, the v-erbA product fails to bind hormone due to mutations in the C-terminal ligand binding domain and thus appears to represent a hormone-independent, oncogenic transcription factor. Therefore, we asked whether or not the C-terminal domain of v-erbA is required for its biological activity and putative transcriptional control functions by analysing mutants with...

Topics

Amino Acid Sequence
Animals
Base Sequence
Blotting, Northern
Cell Division
Cell Transformation, Neoplastic
Chick Embryo
Codon
Fibroblasts
Genes, Regulator
Genetic Variation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Oligonucleotide Probes

Oncogene Proteins v-erbA

Oncogenes

Plasmids

Protein-Tyrosine Kinases

Source

Open in PubMed

Identifiers

PMID: 1969136

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1969136-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Requirement for the C-terminal domain of the v-erbA oncogene protein for biological function and transcriptional repression.PMID 1969136Read ↗

Ontogeny of the v-erbA oncoprotein from the thyroid hormone receptor: an alteration in the DNA binding domain plays a role crucial for v-erbA function.Semantic proximity Read ↗

Mapping of functional domains within the v-erb A oncogene protein: the remnants of the hormone binding domain play multiple, vital roles in protein action.Semantic proximity Read ↗

Mutations in the conserved C-terminal sequence in thyroid hormone receptor dissociate hormone-dependent activation from interference with AP-1 activity.Semantic proximity Read ↗

Multiple mutations contribute to repression by the v-Erb A oncoprotein.Semantic proximity Read ↗

Mutational analysis of the role of the carboxy-terminal region of the v-erbB protein in erythroid cell transformation.Semantic proximity Read ↗

v-erbA oncogene function in neoplasia correlates with its ability to repress retinoic acid receptor action.Semantic proximity Read ↗

v-erbA acts on retinoic acid receptors in immature avian erythroid cells.Semantic proximity Read ↗

Thyroid hormone receptor/and v-erbA. A single amino acid difference in the C-terminal region influences dominant negative activity and receptor dimer formation.Semantic proximity Read ↗

The unique C-termini of the thyroid hormone receptor variant, c-erbA alpha 2, and thyroid hormone receptor alpha 1 mediate different DNA-binding and heterodimerization properties.Semantic proximity Read ↗

The lack of transcriptional activation of the v-erbA oncogene is in part due to a mutation present in the DNA binding domain of the protein.Semantic proximity Read ↗

Mapping C-terminal transactivation domains of the nuclear HER family receptor tyrosine kinase HER3.Semantic proximity Read ↗

The oncoprotein P75gag-v-erbA represses thyroid hormone induced transcription only via response elements containing palindromic half-sites.Semantic proximity Read ↗

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