cAMP-response Element-binding Protein (CREB) Controls MSK1-mediated Phosphorylation of Histone H3 at the c-fos Promoter in Vitro

Shimada, Miho; Nakadai, Tomoyoshi; Fukuda, Aya; Hisatake, Koji

doi:10.1074/jbc.m109.057745

Cited by 33 publications

(25 citation statements)

References 73 publications

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“…Upon BMP-2 addition, we could also detect recruitment of histone H3, phosphorylated at Ser10, into BMP-responsive gene promoters by chromatin immunoprecipitation assays (data not shown). Recently it has been demonstrated that Msk1 should be recruited to responsive promoters by direct interaction with Creb only when phosphorylated at Ser133 (49). Altogether we demonstrate the convergence of Smad and p38 signaling on the activity of specific transcription factors such as Runx2, Atf2, and Creb, that allow the recruitment of coactivators that mediate their effects on Cox2 transcription and likely into other BMP-responsive genes.…”

Section: Discussionmentioning

confidence: 73%

Noncanonical BMP Signaling Regulates Cyclooxygenase-2 Transcription

Susperregui

Gamell

Rodríguez-Carballo

et al. 2011

Molecular Endocrinology

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Activation of p38 MAPK has been shown to be relevant for a number of bone morphogenetic protein (BMP) physiological effects. We report here the involvement of noncanonical phosphorylated mothers against decapentaplegic (Smad) signaling in the transcriptional induction of Cox2 (Ptgs2) by BMP-2 in mesenchymal cells and organotypic calvarial cultures. We demonstrate that different regulatory elements are required for regulation of Cox2 expression by BMP-2: Runt-related transcription factor-2 and cAMP response element sites are essential, whereas a GC-rich Smad binding element is important for full responsiveness. Efficient transcriptional activation requires cooperation between transcription factors because mutation of any element results in a strong decrease of BMP-2 responsiveness. BMP-2 activation of p38 leads to increased recruitment of activating transcription factor-2, Runx2, Smad, and coactivators such as p300 at the responsive sites in the Cox2 proximal promoter. We demonstrate, by either pharmacological or genetic analysis, that maximal BMP-2 effects on Cox2 and JunB expression require the function of p38 and its downstream effector mitogen/stress-activated kinase 1. Altogether our results strongly suggest that cooperative effects between canonical and noncanonical BMP signaling allow the fine-tuning of BMP transcriptional responses on specific target genes.

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Section: Discussionmentioning

confidence: 73%

Noncanonical BMP Signaling Regulates Cyclooxygenase-2 Transcription

Susperregui

Gamell

Rodríguez-Carballo

et al. 2011

Molecular Endocrinology

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“…One possible explanation for these observations is that Nrf2 may directly or indirectly recruit a H3S10 kinase to the HO-1 ARE, where upon the kinase, associated with chromatin, phosphorylates H3S10. This is not without precedence; it has been demonstrated that transcription factors such as c-myc [56], CREB [57], and Elk1 [58] associate with H3S10 kinases on enhancer regions.…”

Section: Discussionmentioning

confidence: 99%

Coordinated regulation of Nrf2 and histone H3 serine 10 phosphorylation in arsenite-activated transcription of the human heme oxygenase-1 gene

Ray

Huang

Tsuji

2015

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

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Expression of the antioxidant gene heme oxygenase-1 (HO-1) is primarily induced through NFE2-related factor 2 (Nrf2)-mediated activation of the antioxidant response element (ARE). Gene transcription is coordinately regulated by transcription factor activity at enhancer elements and epigenetic alterations such as the posttranslational modification of histone proteins. However, the role of histone modifications in the Nrf2-ARE axis remains largely uncharacterized. The environmental contaminant arsenite is a potent inducer of both HO-1 expression and phosphorylation of histone H3 serine 10 (H3S10); therefore, we investigated the relationships between Nrf2 and H3S10 phosphorylation in arsenite-induced, ARE-dependent, transcriptional activation of the human HO-1 gene. Arsenite increased phosphorylation of H3S10 both globally and at the HO-1 promoter concomitantly with HO-1 transcription in human HaCaT keratinocytes. Conversely, arsenite-induced H3S10 phosphorylation and HO-1 expression was blocked by N-acetylcysteine (NAC), the c-Jun N-terminal kinase (JNK) inhibitor SP600125, and JNK knockdown (siJNK). Interestingly, ablation of arsenite-induced H3S10 phosphorylation by SP600125 or siJNK did not inhibit Nrf2 nuclear accumulation nor ARE binding, despite inhibiting HO-1 expression. In response to arsenite, binding of Nrf2 to the HO-1 ARE preceded phosphorylation of H3S10 at the HO-1 ARE. Furthermore, arsenite-mediated occupancy of phosphorylated H3S10 at the HO-1 ARE was decreased in Nrf2-deficient mouse embryonic fibroblasts. These results suggest the involvement of H3S10 phosphorylation in the Nrf2-ARE axis by proposing that Nrf2 may influence H3S10 phosphorylation at the HO-1 ARE and additional promoter regions. Our data highlights the complex interplay between Nrf2 and H3S10 phosphorylation in arsenite-activated HO-1 transcription.

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“…MSK1 and MSK2 activation acts as a feedback control mechanism to dampen the inflammatory response by up-regulating MKP-1 expression through phosphorylation of several transcription factors, including cAMP-response element-binding protein (CREB) and activating transcription factor 1 (ATF1) (35)(36)(37). Therefore, we assessed whether rapamycin also activates MSKs and their downstream transcription factors.…”

Section: Resultsmentioning

confidence: 99%

Rapamycin Induces Mitogen-activated Protein (MAP) Kinase Phosphatase-1 (MKP-1) Expression through Activation of Protein Kinase B and Mitogen-activated Protein Kinase Kinase Pathways

Rastogi

Jiang

Ahmad

et al. 2013

Journal of Biological Chemistry

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Background: MAP kinase phosphatase-1 (MKP-1) plays a critical role in regulating inflammation in innate and adaptive immunity. Results: mTOR inhibition leads to induction of MKP-1 through the activation of AKT1 and MEK1/MEK2 pathways. Rapamycin pretreatment of macrophages inhibits LPS-mediated p38 activation and IL-6 and nitric oxide production. Conclusion: Both AKT1 and MEK1/2 regulate rapamycin-mediated MKP-1 induction. Significance: mTORC1 inhibition regulates immunity through MKP-1 induction.

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cAMP-response Element-binding Protein (CREB) Controls MSK1-mediated Phosphorylation of Histone H3 at the c-fos Promoter in Vitro

Cited by 33 publications

References 73 publications

Noncanonical BMP Signaling Regulates Cyclooxygenase-2 Transcription

Noncanonical BMP Signaling Regulates Cyclooxygenase-2 Transcription

Coordinated regulation of Nrf2 and histone H3 serine 10 phosphorylation in arsenite-activated transcription of the human heme oxygenase-1 gene

Rapamycin Induces Mitogen-activated Protein (MAP) Kinase Phosphatase-1 (MKP-1) Expression through Activation of Protein Kinase B and Mitogen-activated Protein Kinase Kinase Pathways

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