ArticleMolecular and cellular biology1997
Role of hydrophobic amino acid clusters in the transactivation activity of the human glucocorticoid receptor.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 68 citations in OpenAlex.
- Site-specific phosphorylation regulates the structure and function of an intrinsically disordered domain of the glucocorticoid receptor.Scientific reports · 2017Article
- An NMR study on the intrinsically disordered core transactivation domain of human glucocorticoid receptor.BMB reports · 2017Article
- Negative Correlation between the Diffusion Coefficient and Transcriptional Activity of the Glucocorticoid Receptor.International journal of molecular sciences · 2017Article
- A sequence-specific transcription activator motif and powerful synthetic variants that bind Mediator using a fuzzy protein interface.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Determinants of the heightened activity of glucocorticoid receptor translational isoforms.Molecular endocrinology (Baltimore, Md.) · 2013Article
- Nuclear receptors and their selective pharmacologic modulators.Pharmacological reviews · 2013Review
- Pichia pastoris 14-3-3 regulates transcriptional activity of the methanol inducible transcription factor Mxr1 by direct interaction.Molecular microbiology · 2012Article
- Allosteric modulators of steroid hormone receptors: structural dynamics and gene regulation.Endocrine reviews · 2012Review
- Molecular Mechanisms and Genome-Wide Aspects of PPAR Subtype Specific Transactivation.PPAR research · 2010Article
- Glucocorticoid receptor dynamics and gene regulation.Stress (Amsterdam, Netherlands) · 2009Review
- 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
- Structure and function of steroid receptor AF1 transactivation domains: induction of active conformations.The Biochemical journal · 2005Review
- EID3 is a novel EID family member and an inhibitor of CBP-dependent co-activation.Nucleic acids research · 2005Article
- Dual roles of RNA helicase A in CREB-dependent transcription.Molecular and cellular biology · 2001Article
- The role of coactivators and corepressors in the biology and mechanism of action of steroid hormone receptors.Journal of mammary gland biology and neoplasia · 2000Review
- Recruitment of the SWI-SNF chromatin remodeling complex as a mechanism of gene activation by the glucocorticoid receptor tau1 activation domain.Molecular and cellular biology · 2000Article
- Histone acetyltransferase complexes can mediate transcriptional activation by the major glucocorticoid receptor activation domain.Molecular and cellular biology · 1999Article
- Distinct glucocorticoid receptor transcriptional regulatory surfaces mediate the cytotoxic and cytostatic effects of glucocorticoids.Molecular and cellular biology · 1999Article
- Polymorphisms of the glucocorticoid receptor gene in laboratory and wild rats: steroid binding properties of trinucleotide CAG repeat length variants.Mammalian genome : official journal of the International Mammalian Genome Society · 1998Article
- A hydrophobic segment within the 81-amino-acid domain of TFIIIA from Saccharomyces cerevisiae is essential for its transcription factor activity.Molecular and cellular biology · 1998Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have performed a mutagenesis analysis of the 58-amino-acid tau1-core peptide, which represents the core transactivation activity of the tau1 transactivation domain from the glucocorticoid receptor. Mutants with altered activity were identified by phenotypic screening in the yeast Saccharomyces cerevisiae. Most mutants with reduced activity had substitutions of hydrophobic amino acids. Most single-substitution mutants with reduced activity were localized near the N terminus of the tau1-core within a segment that has been shown previously to have a propensity for alpha-helix conformation, suggesting that this helical region is of predominant importance. The particular importance of hydrophobic residues within this region was confirmed by comparing the activities of alanine substitutions of the hydrophobic residues in this and two other helical regions. The hydrophobic residues were shown to be important for the transactivation activity of both the isolated tau1-core and the intact glucocorticoid receptor in mammalian cells. Rare mutations in helical regions I and II gave rise to increased transcriptional activation activity. These mutations increase the hydrophobicity of hydrophobic patches on each of these helices, suggesting a relationship between the hydrophobicity of the patches and transactivation activity. However, certain nonhydrophobic residues are also important for activity. Interestingly, helical region I partially matches a consensus motif found in the retinoic acid receptor, VP16, and several other activator proteins.
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