Activation and repression of the 2-5A synthetase and p21 gene promoters by IRF-1 and IRF-2

Sanit, IT Istituto Superiore di; Coccia, Eliana M.; Russo, Nicoletta Del; Stellacci, Emilia; Orsatti, Roberto; Benedetti, Eleonora; Marziali, Giovanna; Hiscott, John; Battistini, Angela

doi:10.1038/sj.onc.1202536

Cited by 65 publications

(68 citation statements)

References 53 publications

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“…Binding of IRF-1 to these elements promotes transcription (Tanaka et al, 1996;Coccia et al, 1999), whereas binding of IRF-2 to these elements generally represses transcription (Harada et al, 1989;Tanaka et al, 1994;Coccia et al, 1999). Specifically, IRF-2 has been shown to suppress p21 CIP1/WAF1 expression in U937 cells (Coccia et al, 1999;Rubinstein et al, 2000). Thus, the findings of the present study (overexpression of IRF-2 inhibits N-rasG13R-induced growth suppression) support this 'IRF-1-dependent' model of ras-induced growth suppression of myeloid cells.…”

Section: Discussionsupporting

confidence: 75%

“…IRF-2 has been shown to antagonize IRF-1-mediated transcriptional activation (Harada et al, 1989;Coccia et al, 1999). This suggests that IRF-2 expression protects U937 cells from N-rasG13R-induced growth suppression by inhibiting IRF-1-mediated transcription.…”

Section: Mechanism Of Irf-2-mediated Tumor Progressionmentioning

confidence: 87%

“…Both proteins bind to the same DNA promoter elements (interferon regulatory factor-element, IRF-E; interferon-stimulated response element, ISRE) (Harada et al, 1989;Xi and Blanck, 2003). Binding of IRF-1 to these elements promotes transcription (Tanaka et al, 1996;Coccia et al, 1999), whereas binding of IRF-2 to these elements generally represses transcription (Harada et al, 1989;Tanaka et al, 1994;Coccia et al, 1999). Specifically, IRF-2 has been shown to suppress p21 CIP1/WAF1 expression in U937 cells (Coccia et al, 1999;Rubinstein et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

“…This suggested a model for N-rasG13R-induced growth suppression in which N-rasG13R expression induced IRF-1 expression leading in turn to p21 CIP1/WAF1 upregulation and consequent growth arrest. IRF-2 generally antagonizes IRF-1-mediated transcription (Harada et al, 1989;Tanaka et al, 1994;Coccia et al, 1999;Rubinstein et al, 2000). Both proteins bind to the same DNA promoter elements (interferon regulatory factor-element, IRF-E; interferon-stimulated response element, ISRE) (Harada et al, 1989;Xi and Blanck, 2003).…”

Section: Discussionmentioning

confidence: 99%

See 3 more Smart Citations

A retroviral library genetic screen identifies IRF-2 as an inhibitor of N-ras-induced growth suppression in leukemic cells

et al. 2005

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Section: Discussionsupporting

confidence: 75%

Section: Mechanism Of Irf-2-mediated Tumor Progressionmentioning

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

A retroviral library genetic screen identifies IRF-2 as an inhibitor of N-ras-induced growth suppression in leukemic cells

et al. 2005

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“…Through its direct binding to IRF-1, NPM inhibits the transcription regulatory activities of IRF-1 (Kondo et al, 1997). Overexpression of NPM may eliminate the remaining IRF-1 activity, blocking its ability to initiate an apoptotic caspase cascade, and/or induce p21 waf/1cip1 (Coccia et al, 2000) and cooperate with p53 in signaling to growth arrest and apoptosis (Tanaka et al, 1994a(Tanaka et al, , 1996. XBP-1 acts through its ability to regulate genes containing CRE in their promoters (Clauss et al, 1996).…”

Section: One Component Of a Gene Networkmentioning

confidence: 99%

Antiestrogen resistance in breast cancer and the role of estrogen receptor signaling

et al. 2003

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Molecular characterization of Celtix-1, a bromodomain protein interacting with the transcription factor interferon regulatory factor 2

et al. 2000

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Transcriptional control at the G1/S-phase transition of the cell cycle requires functional interactions of multimeric promoter regulatory complexes that contain DNA binding proteins, transcriptional cofactors, and/or chromatin modifying enzymes. Transcriptional regulation of the human histone H4/n gene (FO108) is mediated by Interferon Regulatory Factor-2 (IRF-2), as well as other histone gene promoter factors. To identify proteins that interact with cell-cycle regulatory factors, we performed yeast two-hybrid analysis with IRF-2 and identified a novel human protein termed Celtix-1 which binds to IRF-2. Celtix-1 contains several phylogenetically conserved domains, including a bromodomain, which is found in a number of transcriptional cofactors. Using a panel of IRF-2 deletion mutants in yeast two-hybrid assays, we established that Celtix-1 contacts the C-terminus of IRF-2. Celtix-1 directly interacts with IRF-2 based on binding studies with glutathione S-transferase (GST)/IRF-2 fusion proteins, and immunofluorescence studies suggest that Celtix-1 and IRF-2 associate in situ. Celtix-1 is distributed throughout the nucleus in a heterodisperse pattern. A subset of Celtix-1 colocalizes with the hyperacetylated forms of histones H3 and H4, as well as with the hyperphosphorylated, transcriptionally active form of RNA polymerase II. We conclude that the bromodomain protein Celtix-1 is a novel IRF-2 interacting protein that associates with transcriptionally active chromatin in situ.

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Activation and repression of the 2-5A synthetase and p21 gene promoters by IRF-1 and IRF-2

Cited by 65 publications

References 53 publications

A retroviral library genetic screen identifies IRF-2 as an inhibitor of N-ras-induced growth suppression in leukemic cells

A retroviral library genetic screen identifies IRF-2 as an inhibitor of N-ras-induced growth suppression in leukemic cells

Antiestrogen resistance in breast cancer and the role of estrogen receptor signaling

Molecular characterization of Celtix-1, a bromodomain protein interacting with the transcription factor interferon regulatory factor 2

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