ArticleNucleic acids research1994
Two silencing sub-domains of v-erbA synergize with each other, but not with RXR.
Article in Nucleic acids research, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 15 citations in OpenAlex.
- A novel role for helix 12 of retinoid X receptor in regulating repression.Molecular and cellular biology · 1999Article
- Alien, a highly conserved protein with characteristics of a corepressor for members of the nuclear hormone receptor superfamily.Molecular and cellular biology · 1999Article
- Differential recognition of liganded and unliganded thyroid hormone receptor by retinoid X receptor regulates transcriptional repression.Molecular and cellular biology · 1997Article
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The thyroid hormone receptor (TR) and the retinoic acid receptor (RAR) induce gene expression in the presence of specific ligand and repress transcription in the absence of hormone. This repression is mediated by an active silencing mechanism rather then by interference with DNA binding activators. V-erbA, a variant form of TR which is unable to bind hormone, represents a constitutive repressor. Here we show, using fusion proteins with the GAL4 DNA binding domain, that the minimal silencing domain of v-erbA extends from amino acids 389 to 632 and that internal deletions within this domain retain at least some repression function. Co-transfection experiments of different deletion mutants indicate that the silencing domain is composed of at least two sub-domains which are non-functional when tested individually. When combined in a heterodimeric complex, they synergize such that silencing activity is regained. In contrast to the retinoic acid receptor the retinoid X receptor does not contain a silencing domain. In addition it is unable to cooperate with the repression function of TR or v-erbA in a heterodimer.
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