ArticleMolecular and cellular biology1999
Histone acetyltransferase complexes can mediate transcriptional activation by the major glucocorticoid receptor activation domain.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 63 citations in OpenAlex.
- Tumor Susceptibility Gene 101 Regulates the Glucocorticoid Receptor through Disorder-Mediated Allostery.Biochemistry · 2021Article
- Glucocorticoid Receptor: A Multifaceted Actor in Breast Cancer.International journal of molecular sciences · 2021Review
- Glucocorticoid receptor control of transcription: precision and plasticity via allostery.Nature reviews. Molecular cell biology · 2017Review
- Identification and characterization of BATF3 as a context-specific coactivator of the glucocorticoid receptor.PloS one · 2017Article
- Determinants of the heightened activity of glucocorticoid receptor translational isoforms.Molecular endocrinology (Baltimore, Md.) · 2013Article
- Distinct roles of the Gcn5 histone acetyltransferase revealed during transient stress-induced reprogramming of the genome.BMC genomics · 2013Article
- Human ADA3 regulates RARalpha transcriptional activity through direct contact between LxxLL motifs and the receptor coactivator pocket.Nucleic acids research · 2010Article
- Aging-related gene expression in hippocampus proper compared with dentate gyrus is selectively associated with metabolic syndrome variables in rhesus monkeys.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Human glucocorticoid receptor isoform beta: recent understanding of its potential implications in physiology and pathophysiology.Cellular and molecular life sciences : CMLS · 2009Review
- The loss of histone H3 lysine 9 acetylation due to dSAGA-specific dAda2b mutation influences the expression of only a small subset of genes.Nucleic acids research · 2009Article
- Functional conservation of the glutamine-rich domains of yeast Gal11 and human SRC-1 in the transactivation of glucocorticoid receptor Tau 1 in Saccharomyces cerevisiae.Molecular and cellular biology · 2008Article
- Stress-specific role of fission yeast Gcn5 histone acetyltransferase in programming a subset of stress response genes.Eukaryotic cell · 2006Article
- Methylation of histone H3 mediates the association of the NuA3 histone acetyltransferase with chromatin.Molecular and cellular biology · 2006Article
- ADA3-containing complexes associate with estrogen receptor alpha.Nucleic acids research · 2002Article
- CDP binding to multiple sites in the mouse mammary tumor virus long terminal repeat suppresses basal and glucocorticoid-induced transcription.Journal of virology · 2002Article
- Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo.Molecular and cellular biology · 2001Article
- The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4.Genes & development · 2001Article
- Chromatin remodeling and transcriptional activation: the cast (in order of appearance).Oncogene · 2001Review
- Site-specific acetylation by p300 or CREB binding protein regulates erythroid Krüppel-like factor transcriptional activity via its interaction with the SWI-SNF complex.Molecular and cellular biology · 2001Article
- DAF-16 recruits the CREB-binding protein coactivator complex to the insulin-like growth factor binding protein 1 promoter in HepG2 cells.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previous studies have shown that the Ada adapter proteins are important for glucocorticoid receptor (GR)-mediated gene activation in yeast. The N-terminal transactivation domain of GR, tau1, is dependent upon Ada2, Ada3, and Gcn5 for transactivation in vitro and in vivo. Using in vitro techniques, we demonstrate that the GR-tau1 interacts directly with the native Ada containing histone acetyltransferase (HAT) complex SAGA but not the related Ada complex. Mutations in tau1 that reduce tau1 transactivation activity in vivo lead to a reduced binding of tau1 to the SAGA complex and conversely, mutations increasing the transactivation activity of tau1 lead to an increased binding of tau1 to SAGA. In addition, the Ada-independent NuA4 HAT complex also interacts with tau1. GAL4-tau1-driven transcription from chromatin templates is stimulated by SAGA and NuA4 in an acetyl coenzyme A-dependent manner. Low-activity tau1 mutants reduce SAGA- and NuA4-stimulated transcription while high-activity tau1 mutants increase transcriptional activation, specifically from chromatin templates. Our results demonstrate that the targeting of native HAT complexes by the GR-tau1 activation domain mediates transcriptional stimulation from chromatin templates.
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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.