Protein arginine methyltransferases (PRMTs): Role in chromatin organization

Jahan, Sanzida; Davie, James R.

doi:10.1016/j.jbior.2014.09.003

Cited by 66 publications

(42 citation statements)

References 131 publications

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“…H3K4me3 (Jahan and Davie, 2014). The PRMT catalyzing H3R2me2s is thought to be PRMT5 (a type II PRMT); however, this is not "locked down" at this time.…”

Section: The Recruiters Of the H3k4 Writersmentioning

confidence: 99%

Histone H3K4 trimethylation: dynamic interplay with pre-mRNA splicing

Davie

Delcuve

2016

Biochem. Cell Biol.

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Histone H3 lysine 4 trimethylation (H3K4me3) is often stated as a mark of transcriptionally active promoters. However, closer study of the positioning of H3K4me3 shows the mark locating primarily after the first exon at the 5' splice site and overlapping with a CpG island in mammalian cells. There are several enzyme complexes that are involved in the placement of the H3K4me3 mark, including multiple protein complexes containing SETD1A, SETD1B, and MLL1 enzymes (writers). CXXC1, which is associated with SETD1A and SETD1B, target these enzymes to unmethylated CpG islands. Lysine demethylases (KDM5 family members, erasers) demethylate H3K4me3. The H3K4me3 mark is recognized by several proteins (readers), including lysine acetyltransferase complexes, chromatin remodelers, and RNA bound proteins involved in pre-mRNA splicing. Interestingly, attenuation of H3K4me3 impacts pre-mRNA splicing, and inhibition of pre-mRNA splicing attenuates H3K4me3.

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“…H3K4me3 (Jahan and Davie, 2014). The PRMT catalyzing H3R2me2s is thought to be PRMT5 (a type II PRMT); however, this is not "locked down" at this time.…”

Section: The Recruiters Of the H3k4 Writersmentioning

confidence: 99%

Histone H3K4 trimethylation: dynamic interplay with pre-mRNA splicing

Davie

Delcuve

2016

Biochem. Cell Biol.

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“…That is why cancer therapies now aim at the induction of important silenced genes implicated in cell metabolism by the deactivation of DNMTs or the inhibition of histone deacetylation. This is particularly important in the treatment of hematologic malignancies, where the balance between the hematopoietic stem cell self-renewal and the activation of differentiation processes is modulated by epigenetic mechanisms [3][4][5]. Demethylating drugs specifically target the complex landscape of molecular alterations characterizing the hematologic malignancies to restore a normal hematopoietic differentiation [6,7].…”

Section: Introductionmentioning

confidence: 99%

An increased expression of PI-PLCβ1 is associated with myeloid differentiation and a longer response to azacitidine in myelodysplastic syndromes

Cocco

Finelli

Mongiorgi

et al. 2015

Journal of Leukocyte Biology

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This study tested the hypothesis that PI-PLCβ1 is associated with myeloid differentiation and that its expression could be useful for predicting the response of MDS patients to azacitidine, as the clinical effect of epigenetic treatments is often detectable only after several cycles of therapy. To this end, PI-PLCβ1 was quantified on 70 MDS patients (IPSS risk: 13 Low, 20 Int-1, 31 Int-2, 6 High) at baseline and during the first 3 cycles of azacitidine. Results were then compared with the hematologic response, as assessed after the sixth cycle of azacitidine therapy. Overall, 60 patients completed 6 cycles of azacitidine, and for them, a clinical and molecular evaluation was possible: 37 of these patients (62%) showed a specific increase of PI-PLCβ1 mRNA within the first 3 cycles, which was associated with a longer duration of response and with an increased myeloid differentiation, as evidenced by PI-PLCγ2 induction and the recruitment of specific myeloid-associated transcription factors to the PI-PLCβ1 promoter during azacitidine response. Moreover, the increase of cyclin D3 gene expression throughout all of the therapy showed that PI-PLCβ1-dependent signaling is indeed activated in azacitidine responder patients. Taken together, our results show that PI-PLCβ1 quantification in MDS predicts the response to azacitidine and is associated with an increased myeloid differentiation.

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“…Although PRMT10 and 11 are identified as homologs of PRMT7 and PRMT9, respectively, their physiological roles and functions as methyltransferases are unclear. 14,15) Here, we showed that PRMT10 is abundantly expressed in the prostate and is needed for androgen-dependent proliferation of prostate cancer cells.…”

Section: Discussionmentioning

confidence: 97%

Protein arginine methyltransferase 10 is required for androgen-dependent proliferation of LNCaP prostate cancer cells

Harada

Takagi

Nakano

et al. 2015

Bioscience, Biotechnology, and Biochemistry

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Androgen receptor (AR) signaling is the master regulator of prostate cell growth. Here, to better understand AR signaling, we searched for AR-interacting proteins by yeast two-hybrid screening and identified protein arginine methyltransferase 10 (PRMT10) as one of the interacting proteins. PRMT10 was highly expressed in reproductive tissues, such as prostate. Immunostaining showed that PRMT10 was expressed in the nucleus of both epithelia and stroma of rat prostate. In human prostate cancer LNCaP cells, PRMT10 co-immunoprecipitated with AR in both the presence and absence of dihydrotestosterone (DHT). Knockdown of PRMT10 by siRNA decreased DHT-dependent LNCaP cell growth and induction of prostate-specific antigen, an AR-target gene, without apparent loss of AR. DHT decreased PRMT10 at both the mRNA and protein levels. The decrease in PRMT10 was canceled by knockdown of AR or an AR antagonist. These results indicate that PRMT10 plays an important role in androgen-dependent proliferation of prostate cancer cells.

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Protein arginine methyltransferases (PRMTs): Role in chromatin organization

Cited by 66 publications

References 131 publications

Histone H3K4 trimethylation: dynamic interplay with pre-mRNA splicing

Histone H3K4 trimethylation: dynamic interplay with pre-mRNA splicing

An increased expression of PI-PLCβ1 is associated with myeloid differentiation and a longer response to azacitidine in myelodysplastic syndromes

Protein arginine methyltransferase 10 is required for androgen-dependent proliferation of LNCaP prostate cancer cells

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