CARM1 but not Its Enzymatic Activity Is Required for Transcriptional Coactivation of NF-κB-Dependent Gene Expression

Jayne, Sandrine; Rothgiesser, Karin; Hottiger, Michael O.

doi:10.1016/j.jmb.2009.09.032

Cited by 26 publications

(23 citation statements)

References 40 publications

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“…To our surprise, the enzymatic activity turned out to be dispensable (Supplemental Fig. S8A), as reported recently for the coactivation of NFkB by CARM1 (Jayne et al 2009). Next, we speculated that the cAMP-induced recruitment of CARM1 to ERa is nevertheless necessary for the transcriptional response, and that it might involve a new regulatory or interaction surface on the ERa HBD.…”

Section: Domain Requirements For Signaling Cross-talksupporting

confidence: 83%

CARM1 mediates the ligand-independent and tamoxifen-resistant activation of the estrogen receptor α by cAMP

Carascossa

Dudek²,

Cenni³

et al. 2010

Genes Dev.

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The estrogen receptor a (ERa) is activated as a transcription factor by both estrogen and a large variety of other extracellular signals. The mechanisms of this ligand-independent activation, notably by cAMP signaling, are still largely unknown. We now close the gap in the signaling pathway between cAMP and ERa. Whereas the direct phosphorylation of ERa by the cAMP-activated protein kinase A (PKA) is dispensable, the phosphorylation of the coactivator-associated arginine methyltransferase 1 (CARM1) by PKA at a single serine is necessary and sufficient for direct binding to the unliganded hormone-binding domain (HBD) of ERa, and the interaction is necessary for cAMP activation of ERa. Sustained PKA activity promoting a constitutive interaction may contribute to tamoxifen resistance of breast tumors. Binding and activation involve a novel regulatory groove of the ERa HBD. As a result, depending on the activating signal, ERa recruits different coactivator complexes to regulate alternate sets of target genes.[Keywords: Steroid receptor; signaling; coactivator; protein kinase A; breast cancer; endocrine resistance] Supplemental material is available at http://www.genesdev.org.

show abstract

Section: Domain Requirements For Signaling Cross-talksupporting

confidence: 83%

CARM1 mediates the ligand-independent and tamoxifen-resistant activation of the estrogen receptor α by cAMP

Carascossa

Dudek²,

Cenni³

et al. 2010

Genes Dev.

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show abstract

“…To confirm whether TBBD does the same in ARPE-19 cells, these cells were treated with various concentrations of TBBD for 24 h. As shown in Fig. 5A, 10 lM TBBD decreased and 100 lM TBBD nearly abolished H3R17 dimethylation without affecting histone 3 arginine 26 dimethylation, another substrate of CARM1. However, since treatment with 100 lM TBBD caused cytotoxicity in ARPE-19 cells (data not shown), the cells were challenged with 10 lM TBBD, which attenuated both CARM1-induced and 25 mM glucose-induced cleavages of PARP1 and caspase-3 ( Fig.…”

Section: High-glucose-induced Rpe Cell Apoptosis Is Mediated By Carm1mentioning

confidence: 84%

“…Furthermore, in a previous study, we showed that plant-derived 2,3,7,8-tetrahydroxy(1)-benzopyrano(5,4,3-cde)(1)-benzopyran-5,10-dione (TBBD, ellagic acid), which is a specific inhibitor of CARM1-induced histone 3 arginine 17 (H3R17) dimethylation, represses the binding of H3R17 to the p53-responsive site within the p21 promoter [9]. As a transcriptional cofactor, CARM1 also increased the transcriptional activity of nuclear factor kappa B (NF-jB) [10,11]. Even though CARM1 can regulate p53 and NF-jB, which are closely associated with RPE cell apoptosis [12,13], its regulation of apoptosis in RPE cells has not been elucidated.…”

Section: Introductionmentioning

confidence: 99%

High-glucose-induced CARM1 expression regulates apoptosis of human retinal pigment epithelial cells via histone 3 arginine 17 dimethylation: Role in diabetic retinopathy

Kim¹,

Park²,

Lim³

et al. 2014

Archives of Biochemistry and Biophysics

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“…The custom array analysis was subsequently performed as previously described (29). Briefly, RNA was processed with the Amino Allyl MessageAMP II aRNA Amplification Kit (Ambion) according to the manufacturer's instructions to yield aminoallyl-modified aRNA that was further coupled to Cy3 or Cy5 dyes, respectively.…”

Section: Methodsmentioning

confidence: 99%

The Peroxisome Proliferator-activated Receptor γ Coactivator 1α/β (PGC-1) Coactivators Repress the Transcriptional Activity of NF-κB in Skeletal Muscle Cells

Eisele

Salatino

Sobek

et al. 2013

Journal of Biological Chemistry

Self Cite

162

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Background: Peroxisome proliferator-activated receptor ␥ coactivator 1 (PGC) ␣ and PGC-1␤ are metabolic coactivators that are dysregulated in muscle in many chronic diseases. Results: PGC-1␣ and PGC-1␤ differentially suppress expression of proinflammatory cytokines induced by various stimuli. Conclusion: In muscle cells, PGC-1␣ and PGC-1␤ modulate the NF-B pathway thus profoundly affecting inflammatory processes. Significance: Targeting PGC-1␣ and PGC-1␤ in chronic diseases might reduce inflammation and thereby reverse disease progression.

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CARM1 but not Its Enzymatic Activity Is Required for Transcriptional Coactivation of NF-κB-Dependent Gene Expression

Cited by 26 publications

References 40 publications

CARM1 mediates the ligand-independent and tamoxifen-resistant activation of the estrogen receptor α by cAMP

CARM1 mediates the ligand-independent and tamoxifen-resistant activation of the estrogen receptor α by cAMP

High-glucose-induced CARM1 expression regulates apoptosis of human retinal pigment epithelial cells via histone 3 arginine 17 dimethylation: Role in diabetic retinopathy

The Peroxisome Proliferator-activated Receptor γ Coactivator 1α/β (PGC-1) Coactivators Repress the Transcriptional Activity of NF-κB in Skeletal Muscle Cells

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