v-erbA oncogene activation entails the loss of hormone-dependent regulator activity of c-erbA 

@article{Zenke1990verbAOA,
  title={v-erbA oncogene activation entails the loss of hormone-dependent regulator activity of c-erbA
},
  author={Martin Zenke and Alberto Mu{\~n}oz and Jan Sap and Björn Vennström and Hartmut Beug},
  journal={Cell},
  year={1990},
  volume={61},
  pages={1035-1049}
}
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204 Citations
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13
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204 Citations

Transcriptional regulation by v-ErbA, the oncogenic counterpart of thyroid hormone receptor (TR)
TLDR
The data suggest that v-ErbA prevents CA II activation by ‘neutralizing’ in cis the activity of erythroid transcription factors.
v-erbA overexpression is required to extinguish c-erbA function in erythroid cell differentiation and regulation of the erbA target gene CAII.
TLDR
It is shown that v-erbA and c-erb a bind directly to sequences within the promoter of the erythrocyte-specific carbonic anhydrase II (CAII), a gene whose transcription is efficiently suppressed by v- DerbA.
Phosphorylation of the v-erbA protein is required for its function as an oncogene.
TLDR
The hypothesis that phosphorylation of the gag/v-erbA protein is important for transcriptional repression of at least some of its target genes in erythroid cells is supported.
The v-ErbA oncoprotein quenches the activity of an erythroid-specific enhancer
TLDR
It is proposed that depending on the sequence and context of the binding site, v-ErbA contributes to leukomogenesis by occluding liganded TR as well as unliganded TR thereby preventing activation or repression, respectively.
Multiple mutations contribute to repression by the v-Erb A oncoprotein
TLDR
It is proposed that the acquisition of oncogenic potential by the v-Erb A protein was a multistep process involving a series of mutations that alter the transcriptional repressive properties of the viral protein through multiple mechanisms.
The v‐erbA Oncoprotein of the AEV Transforming Retrovirus Binds to the Promoter Region of the Erythroid‐specific Band 3 Gene
Avian erythroblastosis virus (AEV) which carries two oncogenes, v-erbA and verbR. causes erythroleukemia and sarcomas in young chickens and transforms embryo fibroblasts and bone marrow cells in…
v-erbA Oncogene function in neoplasia correlates with its ability to repress retinoic acid receptor action
Functional interaction between the two zinc finger domains of the v-erb A oncoprotein.
TLDR
It is reported here that alteration of the sequence at threonine 78 such that it resembles that of c-erb A can act as an intragenic suppressor and can partially restore function to a v-erb B protein rendered defective due to a mutation at position 61.
A conserved C-terminal sequence that is deleted in v-ErbA is essential for the biological activities of c-ErbA (the thyroid hormone receptor)
TLDR
It is concluded 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.
Thyroid Hormone Receptor / c-erbA : Control of Commitment and Differentiation in the Neuronal / Chromatfin Progenitor Line PC 12
TLDR
Results suggest that TRet-1 plays an important role in regulating commitment and maturation of neuronal progenitors and the finding that TRo~-I constitutively blocked dexamethasone-induced differentiation of PC12 cells into the chromaffin pathway is suggested.
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References

SHOWING 1-10 OF 68 REFERENCES
Repression of transcription mediated at a thyroid hormone response element by the v-erb-A oncogene product
TLDR
The data indicate that overexpressed v-erb-A protein negatively interferes with normal transcriptional-control mechanisms, and that amino-acid substitutions have altered its DNA-binding properties.
v-erbA specifically suppresses transcription of the avian erythrocyte anion transporter (Band 3) gene
Genetic dissection of functional domains within the avian erythroblastosis virus v-erbA oncogene
TLDR
The results suggest that the mechanism of action of the v-erbA protein in establishing the neoplastic phenotype is closely related to its ability to interact with DNA, presumably thereby altering expression of host target genes by either mimicking or interfering with theaction of the normal c-erbB gene product.
Expression of the v-erbA product, an altered nuclear hormone receptor, is sufficient to transform erythrocytic cells in vitro
The avian erythroblastosis virus erbA oncogene encodes a DNA-binding protein exhibiting distinct nuclear and cytoplasmic subcellular localizations
TLDR
The protein product of the v-erbA oncogene of avian erythroblastosis virus was analyzed by use of site-specific antisera and found to exist in distinct nuclear and cytoplasmic forms.
A novel thyroid hormone receptor encoded by a cDNA clone from a human testis library.
TLDR
It is shown that the erbA-T protein binds specifically to 3,5,3'-triiodo-L-thyronine with a dissociation constant of 3.8 +/- 0.2 x 10(-10) M, implying that more than one thyroid hormone receptor exists in humans and that these receptors might have different tissue- and gene-activating specificities.
c-erbA encodes multiple proteins in chicken erythroid cells
TLDR
The results indicate that posttranscriptional or translational mechanisms are involved in regulation of c-erbA expression and in the complexity of its protein products.
v-erbA cooperates with sarcoma oncogenes in leukemic cell transformation
Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonist
TLDR
The oncogenic derivative of the thyroid-hormone receptor, v-erbA, acts as a constitutive represser and, when coexpressed with the receptor, blocks activation by thyroid hormone.
Dual regulatory role for thyroid-hormone receptors allows control of retinoic-acid receptor activity
TLDR
It is found that RAR-ε is very efficient at inducing transcription from two distinct thyroid-hormone responsive elements (TREs) and may have dual regulatory roles: in the presence of hormone they function as TRE-specific transcriptional activators; in the absence of hormone, however, they can function as Tre-specific repressers.
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