Recruitment of CBP/p300 by the IFNβ Enhanceosome Is Required for Synergistic Activation of Transcription

Merika, Menie; Williams, Amy J.; Chen, Guoying; Collins, Tucker; Thanos, Dimitris

doi:10.1016/s1097-2765(00)80028-3

Cited by 417 publications

(397 citation statements)

References 39 publications

(12 reference statements)

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“…Similar conclusions were drawn for the well-studied b-interferon enhanceosome (Merika et al, 1998). Although the ability of an NF-kB dimer to bind DNA is a requirement for gene activation, it is not sufficient for activation.…”

Section: Transcriptional Specificity Of Nf-jb As Determined By Molecusupporting

confidence: 74%

Transcriptional regulation via the NF-κB signaling module

2006

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Stimulus-induced nuclear factor-jB (NF-jB) activity, the central mediator of inflammatory responses and immune function, comprises a family of dimeric transcription factors that regulate diverse gene expression programs consisting of hundreds of genes. A family of inhibitor of jB (IjB) proteins controls NF-jB DNA-binding activity and nuclear localization. IjB protein metabolism is intricately regulated through stimulus-induced degradation and feedback re-synthesis, which allows for dynamic control of NF-jB activity. This network of interactions has been termed the NF-jB signaling module. Here, we summarize the current understanding of the molecular structures and biochemical mechanisms that determine NF-jB dimer formation and the signal-processing characteristics of the signaling module. We identify NF-jB-jB site interaction specificities and dynamic control of NF-jB activity as mechanisms that generate specificity in transcriptional regulation. We discuss examples of gene regulation that illustrate how these mechanisms may interface with other transcription regulators and promoter-associated events, and how these mechanisms suggest regulatory principles for NF-jB-mediated gene activation.

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Section: Transcriptional Specificity Of Nf-jb As Determined By Molecusupporting

confidence: 74%

Transcriptional regulation via the NF-κB signaling module

2006

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“…Phosphorylated CREB recruits p300 and CBP and binds to the Ϫ180 (9) and possibly other sites on the IL-2 promoter (31). The binding of other factors like AP1 and NF-B together with pCREB and their ability to recruit CBP and p300 lead to the building of an enhanceosome that associates with the RNA polymerase II complex (32)(33)(34) and activates the transcription of IL-2 mRNA and the production of protein. The binding of pCREB declines after 2-6 h promoted by increased dephosphorylation by phosphatases PP1 and PPA2 (35).…”

Section: Discussionmentioning

confidence: 99%

The Cyclic Adenosine 5′-Monophosphate Response Element Modulator Suppresses IL-2 Production in Stimulated T Cells by a Chromatin-Dependent Mechanism

Tenbrock

Juang

Tolnay

et al. 2003

The Journal of Immunology

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The production of IL-2 is tightly controlled by several transcription factors that bind to the IL-2 promoter. The cAMP response element modulator (CREM) is known to form complexes with CREB and bind to the −180 site of the IL-2 promoter in anergic and in systemic lupus erythematosus T cells. In this study we show that CREM is transcriptionally induced in T cells following stimulation through CD3 and CD28, binds to the IL-2 promoter in vivo, and suppresses IL-2 production. Transfection of an antisense CREM plasmid into T cells blocked the expression and binding of CREM to the IL-2 promoter and the decrease of IL-2 production, which follows the early increase after T cell stimulation with CD3 and CD28. In addition, as assessed by chromatin immunoprecipitation experiments, antisense CREM prevented the binding of protein 300 and cAMP response element binding protein and promoted the acetylation of histones. Antisense CREM also enhanced the accessibility of the IL-2 promoter to endonucleases and prevented the condensation of chromatin in vivo. Our data suggest that upon T cell activation, CREM gradually replaces phosphorylated CREB at the −180 site of the IL-2 promoter. CREM, in turn, binds protein 300 and cAMP response element binding protein, but CREM is unable to activate its histone acetyltransferase activity, which results in condensation of chromatin and down-regulation of IL-2 production.

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“…One possible explanation for these results may be that the factors binding the ERBB2 enhancer may provide a common interaction surface which allows them collectively to recruit SRC-1. Such a strategy is believed to be used by the so-called enhanceosome of interferon (IFN)-b in the recruitment of p300/ CBP during transcriptional activation of the gene (Merika et al, 1998) and has also been proposed to contribute to the functioning of other enhancers (Carey, 1998).…”

Section: Discussionmentioning

confidence: 99%

Cofactor competition between the ligand-bound oestrogen receptor and an intron 1 enhancer leads to oestrogen repression of ERBB2 expression in breast cancer

et al. 2000

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Overexpression of the ERBB2 proto-oncogene in breast tumours, which occurs in 25 ± 30% of patients, correlates with poor prognosis. In oestrogen receptor (ER) positive breast epithelial cells oestrogens reduce ERBB2 mRNA and protein levels, an e ect that is reversed in the presence of anti-oestrogens such as tamoxifen and ICI 182780. Our previous studies have shown that the major e ect of oestrogen on ERBB2 expression is at the level of transcription and that this is mediated through a region within the ERBB2 ®rst intron which can act as an oestrogen-suppressible enhancer in ER positive breast cells. In vitro footprinting of the smallest DNA fragment that retained full activity revealed four transcription factor binding sites. We report here that two of these sites are recognized by AP-2 proteins and the other two are bound by a variety of bZIP factors, including CREB and ATF1, with a major complex containing ATFa/ JunD. However, by using ER mutants it is clear that repression occurs essentially o the DNA. Indeed, the essential domain of the ER responsible for repression of the ERBB2 enhancer is a region termed AF2 which is required for the ligand-dependent association of non-DNA binding cofactors. We further demonstrate that one of these ER cofactors, SRC-1, can relieve oestrogen repression of the ERBB2 enhancer and conclude that these data ®t with a model whereby the ER and the ERBB2 enhancer compete for this limiting, non-DNA binding cofactor. Thus, in oestrogenic conditions SRC-1 preferentially binds to the ER which e ectively sequesters it thereby reducing enhancer activity, but in antioestrogenic media the cofactor is released from the ER and is therefore available to activate the ERBB2 enhancer. Oncogene (2000) 19, 490 ± 497.

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Recruitment of CBP/p300 by the IFNβ Enhanceosome Is Required for Synergistic Activation of Transcription

Cited by 417 publications

References 39 publications

Transcriptional regulation via the NF-κB signaling module

Transcriptional regulation via the NF-κB signaling module

The Cyclic Adenosine 5′-Monophosphate Response Element Modulator Suppresses IL-2 Production in Stimulated T Cells by a Chromatin-Dependent Mechanism

Cofactor competition between the ligand-bound oestrogen receptor and an intron 1 enhancer leads to oestrogen repression of ERBB2 expression in breast cancer

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