ArticleNucleic acids research1998
Multiple receptor interaction domains of GRIP1 function in synergy.
Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- A mechanism for pituitary-resistance to thyroid hormone (PRTH) syndrome: a loss in cooperative coactivator contacts by thyroid hormone receptor (TR)beta2.Molecular endocrinology (Baltimore, Md.) · 2011Article
- The p160 coactivator PAS-B motif stabilizes nuclear receptor binding and contributes to isoform-specific regulation by thyroid hormone receptors.The Journal of biological chemistry · 2009Article
- Gene interaction network suggests dioxin induces a significant linkage between aryl hydrocarbon receptor and retinoic acid receptor beta.Environmental health perspectives · 2004Article
- Human immunodeficiency virus type 1 Vpr contains two leucine-rich helices that mediate glucocorticoid receptor coactivation independently of its effects on G(2) cell cycle arrest.Journal of virology · 2000Article
- Article
- The androgen receptor amino-terminal domain plays a key role in p160 coactivator-stimulated gene transcription.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
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear hormone receptors are exerting their effect on transcription by interacting with basal factors of the transcription machinery and/or by recruiting intermediary factors, such as the mouse protein GRIP1. GRIP1 is one of the recently identified coactivators for nuclear hormone receptors. Upon interaction with the hormone-binding domain of the receptors, GRIP1 increases their transcriptional activity. Here we show that GRIP1 contains at least two receptor-interacting regions using the hormone-binding domain of several receptors as bait in the yeast two-hybrid assay. GRIP1 interacts in a hormone-dependent manner with the C-termini of nuclear hormone receptors such as GRalpha, TRalpha, TRbeta, RARalpha and RXRalpha but not with v-ErbA. GRIP1 contains several LXXLL motifs which were shown to be required for receptor interaction. A protein fragment containing all of the three LXXLL motifs, but having the activation domain deleted, is able to repress the transcriptional activity of human TRbeta, whereas a region harbouring only one LXXLL motif fails to do so. A protein fragment with two LXXLL motifs exhibits an intermediate modulation of the TRbeta transactivation. While one motif seems to be sufficient for receptor interaction, more than one motif is needed for functional interference.
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Registered trials
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.