Recruitment of the SWI-SNF Chromatin Remodeling Complex as a Mechanism of Gene Activation by the Glucocorticoid Receptor τ1 Activation Domain

Wallberg, Annika E.; Neely, Kristen E.; Hassan, Ahmed H.E.; Gustafsson, Jan‐Åke; Workman, Jerry L.; Wright, Anthony P. H.

doi:10.1128/mcb.20.6.2004-2013.2000

Cited by 122 publications

(93 citation statements)

References 51 publications

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“…On MMTV LTR DNA reconstituted into polynucleosome arrays with Drosophila embryo extracts, puri®ed GR required ATP and HeLa nuclear extract to induce chromatin remodeling (Fletcher et al, 2000). Yeast Swi/Snf stimulated transcription via the N-terminal transactivation domain of the GR, tl, from assembled chromatin templates (Wallberg et al, 2000). In the same report, BRM potentiated tl-dependent activation of a transiently introduced glucocorticoid-responsive promoter in human cervical carcinoma cells.…”

Section: Gr and Chromatin-remodeling Complexesmentioning

confidence: 52%

Glucocorticoid receptor-mediated chromatin remodeling in vivo

Deroo

Archer

2001

Oncogene

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The compaction of DNA into chromatin provides an additional level of gene regulation in eukaryotes that may not be available to prokaryotes. When packaged as chromatin, most promoters are transcriptionally repressed, and transcription factors have reduced access to their binding sites. The glucocorticoid receptor (GR) is a ligand-activated transcription factor that regulates the activity of genes involved in many physiological processes. To regulate eukaryotic genes, the GR binds to target sites within promoter regions of genes assembled as chromatin. This interaction alters the nucleosomal architecture to allow binding of other transcription factors, and formation of the preinitiation complex. The mouse mammary tumor virus (MMTV) promoter has been used extensively as a model to explore the processes by which the GR remodels chromatin and activates transcription. Signi®cant progress has been made in our understanding of the mechanisms used by the GR to modify chromatin structure, and the limits placed on the GR by post-translational modi®cations of histones. We will describe recent developments in the processes used by the GR to activate transcription in vivo via chromatin remodeling complexes, histone H1 phosphorylation, and recruitment of diverse coactivators. Oncogene (2001) 20, 3039 ± 3046.

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Section: Gr and Chromatin-remodeling Complexesmentioning

confidence: 52%

Glucocorticoid receptor-mediated chromatin remodeling in vivo

Deroo

Archer

2001

Oncogene

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“…These results suggest that SRG3 may modulate the sensitivity to GC-induced apoptosis by directly regulating the transcriptional activity of GR. In addition, it has been also shown that GR physically interacts with the SWI/SNF complex, and trans-activation of GR requires Brg1/BAF chromatin remodeling complex (29,50). Whether SRG3 affects the transcriptional activity of GR independently or as a component of SWI/SNF complex remains to be elucidated.…”

Section: Discussionmentioning

confidence: 99%

T Cell Receptor Signaling Inhibits Glucocorticoid-induced Apoptosis by Repressing the SRG3 Expression via Ras Activation

Jang

Ahn

et al. 2004

Journal of Biological Chemistry

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“…7A). This model may also explain mechanisms of potential interference with p300 activity by SYT-SSX (23). Second, SSX1C recruits the SNF/SWI complexes to aberrant target sites by interacting with modified chromatin (e.g.…”

Section: Possible Molecular Mechanisms Of Malignant Transformation Bymentioning

confidence: 99%

SYT Associates with Human SNF/SWI Complexes and the C-terminal Region of Its Fusion Partner SSX1 Targets Histones

Kato¹,

Tjernberg²,

Zhang³

et al. 2002

Journal of Biological Chemistry

100

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A global transcriptional co-activator, the SNF/SWI complex, has been characterized as a chromatin remodeling factor that enhances accessibility of the transcriptional machinery to DNA within a repressive chromatin structure. On the other hand, mutations in some human SNF/SWI complex components have been linked to tumor formation. We show here that SYT, a partner protein generating the synovial sarcoma fusion protein SYT-SSX, associates with native human SNF/SWI complexes. The SYT protein has a unique QPGY domain, which is also present in the largest subunits, p250 and the newly identified homolog p250R, of the corresponding SNF/SWI complexes. The C-terminal region (amino acids 310 -387) of SSX1, comprising the SSX1 portion of the SYT-SSX1 fusion protein, binds strongly to core histones and oligonucleosomes in vitro and directs nuclear localization of a green fluorescence protein fusion protein. Experiments with serial C-terminal deletion mutants of SSX1 indicate that these properties map to a common region and also correlate with the previously demonstrated anchorage-independent colony formation activity of SYT-SSX in Rat 3Y1 cells. These data suggest that SYT-SSX interferes with the function of either the SNF/SWI complexes or another SYT-interacting co-activator, p300, by changing their targeted localization or by directly inhibiting their chromatin remodeling activities.The chromatin structure of active eukaryotic genes is subject to dynamic change by chromatin modifiers such as ATP-dependent chromatin remodeling factors (reviewed in Refs. 1-5). Homologs of a yeast prototype ATP-dependent remodeling complex, SNF/SWI, appear to be widely present in eukaryotes from yeast to humans (6 -8). Functions of the subunits of the SNF/ SWI complexes (9, 10) were first demonstrated by genetic studies in Saccharomyces cerevisiae, which showed that SWI1/ ADR6, SWI2/SNF2, SWI3, and SNF5 are required for the expression of a set of genes that include the HO, GAL1, SUC2, and ADH2 genes (11-13). In Drosophila melanogaster, the SWI2/SNF2 homolog brm was originally identified as a suppressor of Polycomb mutations (14). The Drosophila complex has been isolated, and some of the subunits have been characterized (15, 16), revealing that the SNF/SWI complexes are highly conserved in subunit composition and in primary structure among yeast, fruit fly, and human. A number of studies have described various biochemical properties of the human and yeast SNF/SWI complexes, as well as other ATP-dependent chromatin remodeling complexes (reviewed in Refs. 1-3, 17). For instance the SNF/SWI complexes are recruited by transcriptional activators to nucleosomal templates (18 -23), perturb nucleosome positioning, and facilitate binding of activator proteins to nucleosomes (24 -26). Mechanisms for this perturbation have been proposed to involve interconversion between two different nucleosomal states (27), sliding of histone octamers (28) or a change of DNA topology (29, 30).The human complexes are composed of at least nine subunits that include appar...

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Recruitment of the SWI-SNF Chromatin Remodeling Complex as a Mechanism of Gene Activation by the Glucocorticoid Receptor τ1 Activation Domain

Cited by 122 publications

References 51 publications

Glucocorticoid receptor-mediated chromatin remodeling in vivo

Glucocorticoid receptor-mediated chromatin remodeling in vivo

T Cell Receptor Signaling Inhibits Glucocorticoid-induced Apoptosis by Repressing the SRG3 Expression via Ras Activation

SYT Associates with Human SNF/SWI Complexes and the C-terminal Region of Its Fusion Partner SSX1 Targets Histones

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