Methylation of Histone H4 at Arginine 3 Facilitating Transcriptional Activation by Nuclear Hormone Receptor

Wang, Hengbin; Huang, Zhiqing; Li, Xia; Feng, Qin; Erdjument‐Bromage, Hediye; Strahl, Brian D.; Briggs, Scott; Allis, C. David; Wong, Jiemin; Tempst, Paul; Zhang, Yi

doi:10.1126/science.1060781

Cited by 691 publications

(664 citation statements)

References 18 publications

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“…There are three related 160-kDa proteins, SRC-1 (steroid receptor co-activator-1), TIF-2 (transcriptional intermediary factor) and RAC3 (receptor-associated co-activator-3), encoded by separate genes, which form the SRC or p160 family of co-activators (Xu and Qingtian, 2003). The molecular mechanism by which co-activators exert the chromatin remodeling and transcriptional activation involves the histone acetyltransferase activity that SRC-1 and RAC3 have at their C-terminal domain (Spencer et al, 1997;Glass and Rosenfeld, 2000) such as the recruitment of other general co-activators with enzymatic activity like CBP (CREB-binding protein)/p300, p/CAF, CARM-1 and PRMT1 (Chen et al, 1999;Wang et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

The p160 nuclear receptor co-activator RAC3 exerts an anti-apoptotic role through a cytoplasmatic action

et al. 2007

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The p160 nuclear receptor co-activators represent a family of molecules, which are recruited by steroid nuclear receptors as well as other transcription factors that are overexpressed in several tumors. We investigated the role of one member of this family on the sensitivity of cells to apoptosis. We observed that overexpression of the RAC3 (receptor-associated co-activator-3) p160 co-activator inhibits hydrogen peroxide-induced cell death in human embryonic kidney 293 (HEK293) cells. The mechanism involves the activation of anti-apoptotic pathways mediated through enhanced nuclear factor kappa B (NFjB) activity, inhibition of caspase-9 activation, diminished apoptotic-inducing factor (AIF) nuclear localization and a change in the activation pattern of several kinases, including an increase in both AKT and p38 kinase activities, and inhibition of ERK2. Moreover, RAC3 has been found associated with a protein complex containing AIF, Hsp90 and dynein, suggesting a role for the coactivator in the cytoplasmatic nuclear transport of these proteins associated with cytoskeleton. These results demonstrate that there are several molecular pathways that could be affected by their overexpression, including those not restricted to steroid regulation or the nuclear action of co-activators, which results in diminished sensitivity to apoptosis. Furthermore, this could represent one mechanism by which co-activators contribute to tumor development.

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Section: Introductionmentioning

confidence: 99%

The p160 nuclear receptor co-activator RAC3 exerts an anti-apoptotic role through a cytoplasmatic action

et al. 2007

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“…phosphate, acetyl, or methyl) to specific amino acid residues (1), which play important roles in regulating gene expression, modifying protein functions, and modulating protein-protein interactions (2)(3)(4)(5)(6). With the development of mass spectrometry (MS) techniques, increasing number of PTM sites have been identified (7,8).…”

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Systematic Characterization and Prediction of Post-Translational Modification Cross-Talk *

Huang

Xu²,

Zhou

et al. 2015

Molecular & Cellular Proteomics

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Post-translational modification (PTM) 1 plays an important role in regulating the functions of proteins. PTMs of multiple residues on one protein may work together to determine a functional outcome, which is known as PTM crosstalk. Identification of PTM cross-talks is an emerging theme in proteomics and has elicited great interest, but their properties remain to be systematically characterized. To this end, we collected 193 PTM cross-talk pairs in 77 human proteins from the literature and then tested location preference and co-evolution at the residue and modification levels. We found that cross-talk events preferentially occurred among nearby PTM sites, especially in disordered protein regions, and cross-talk pairs tended to co-evolve. Given the properties of PTM cross-talk pairs, a naïve Bayes classifier integrating different features was built to predict cross-talks for pairwise combination of PTM sites. By using a 10-fold cross-validation, the integrated prediction model showed an area under the receiver operating characteristic (ROC) curve of 0.833, superior to using any individual feature alone. The prediction performance was also demonstrated to be robust to the biases in the collected PTM cross-talk pairs. The integrated approach has the potential for large-scale prioritization of PTM cross-talk candidates for functional validation and was implemented as a web server available at

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“…Thereinto, PRMT1, belonging to type I enzymes, participates in a variety of cellular processes including signal transduction, epigenetic regulation, and DNA repair pathways (11,12). PRMT1, on the one hand, can catalyze the methylation of histones H4 at arginine 3 (H4R3), which acts as a part of the histone code to regulate gene expression (11)(12)(13); on the other hand, recent studies have revealed that a plethora of proteins with methylated arginine residues catalyzed by PRMT1 implicate in a variety of cellular processes. For example, PRMT1 enhances gene transcription by methylating N-terminal arginine residues in NFAT-interacting protein 45, which heterodimerizes with NFAT and then enhances NFAT, driving cytokine production upon TCR signaling of T cells (14,15).…”

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confidence: 99%

Upregulated Protein Arginine Methyltransferase 1 by IL-4 Increases Eotaxin-1 Expression in Airway Epithelial Cells and Participates in Antigen-Induced Pulmonary Inflammation in Rats

Sun

Yang

Zhong

et al. 2012

The Journal of Immunology

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Protein arginine methyltransferases (PRMTs), catalyzing methylation of both histones and other cellular proteins, have emerged as key regulators of various cellular processes. This study aimed to identify key PRMTs involved in Ag-induced pulmonary inflammation (AIPI), a rat model for asthma, and to explore the role of PRMT1 in the IL-4–induced eosinophil infiltration process. E3 rats were i.p. sensitized with OVA/alum and intranasally challenged with OVA to induce AIPI. The expressions of PRMT1–6, eotaxin-1, and CCR3 in lungs were screened by real-time quantitative PCR. Arginine methyltransferase inhibitor 1 (AMI-1, a pan-PRMT inhibitor) and small interfering RNA–PRMT1 were used to interrupt the function of PRMT1 in A549 cells. In addition, AMI-1 was administrated intranasally to AIPI rats to observe the effects on inflammatory parameters. The results showed that PRMT1 expression was mainly expressed in bronchus and alveolus epithelium and significantly upregulated in lungs from AIPI rats. The inhibition of PRMTs by AMI-1 and the knockdown of PRMT1 expression were able to downregulate the expressions of eotaxin-1 and CCR3 with the IL-4 stimulation in the epithelial cells. Furthermore, AMI-1 administration to AIPI rats can also ameliorate pulmonary inflammation, reduce IL-4 production and humoral immune response, and abrogate eosinophil infiltration into the lungs. In summary, PRMT1 expression is upregulated in AIPI rat lungs and can be stimulated by IL-4. Intervention of PRMT1 activity can abrogate IL-4–dependent eotaxin-1 production to influence the pulmonary inflammation with eosinophil infiltration. The findings may provide experimental evidence that PRMT1 plays an important role in asthma pathogenesis.

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Methylation of Histone H4 at Arginine 3 Facilitating Transcriptional Activation by Nuclear Hormone Receptor

Cited by 691 publications

References 18 publications

The p160 nuclear receptor co-activator RAC3 exerts an anti-apoptotic role through a cytoplasmatic action

The p160 nuclear receptor co-activator RAC3 exerts an anti-apoptotic role through a cytoplasmatic action

Systematic Characterization and Prediction of Post-Translational Modification Cross-Talk *

Upregulated Protein Arginine Methyltransferase 1 by IL-4 Increases Eotaxin-1 Expression in Airway Epithelial Cells and Participates in Antigen-Induced Pulmonary Inflammation in Rats

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