PRMT2, a member of the protein arginine methyltransferase family, is a coactivator of the androgen receptor

Meyer, René; Wolf, Siegmund S.; Obendorf, Maik

doi:10.1016/j.jsbmb.2007.05.006

Cited by 82 publications

(85 citation statements)

References 56 publications

(87 reference statements)

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“…S3A). In most cases, these localizations were in line with earlier reports (Frankel et al, 2002;Lee et al, 2005a;Meyer et al, 2007;Rho et al, 2001;Tang et al, 1998), but especially in the case of PRMT1 and CARM1/PRMT4 there was some discrepancy that we wanted to investigate further. We hypothesized that the localization could be cell-type specific, and created stable cell lines for PRMT1v2 and CARM1/PRMT4 from often-used parental cell lines U2OS, HeLa and MCF7.…”

Section: Localization Of Prmt-gfp Fusion Proteins In Live Cellssupporting

confidence: 88%

“…In a second step, the type I enzymes PRMT1 (Lin et al, 1996), PRMT3 (Tang et al, 1998), CARM1/PRMT4 (Chen et al, 1999), PRMT6 (Frankel et al, 2002) and PRMT8 (Lee et al, 2005a;Sayegh et al, 2007) lead to the formation of asymmetric dimethylarginine, whereas the type II enzyme PRMT5 (Branscombe et al, 2001;Pollack et al, 1999) and possibly PRMT7 (Lee et al, 2005b;Miranda et al, 2004) lead to symmetric dimethylarginine. One more member of the PRMT family, PRMT2, was identified by sequence homology to the known enzymes (Katsanis et al, 1997), but has not been classified into a group, because no enzymatic activity has yet been demonstrated or substrates identified; nevertheless, PRMT2 acts as a coactivator in hormonedependent gene expression (Meyer et al, 2007;Qi et al, 2002). Recently, an additional arginine methyltransferase activity has been described for FBXO11 (Cook et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

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Human protein arginine methyltransferases in vivo – distinct properties of eight canonical members of the PRMT family

Herrmann

Pably

Eckerich

et al. 2009

Journal of Cell Science

129

114

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Methylation of arginine residues is a widespread post-translational modification of proteins catalyzed by a small family of protein arginine methyltransferases (PRMTs). Functionally, the modification appears to regulate protein functions and interactions that affect gene regulation, signalling and subcellular localization of proteins and nucleic acids. All members have been, to different degrees, characterized individually and their implication in cellular processes has been inferred from characterizing substrates and interactions. Here, we report the first comprehensive comparison of all eight canonical members of the human PRMT family with respect to subcellular localization and dynamics in living cells. We show that the individual family members differ significantly in their properties, as well as in their substrate specificities, suggesting that they fulfil distinctive, non-redundant functions in vivo. In addition, certain PRMTs display different subcellular localization in different cell types, implicating cell- and tissue-specific mechanisms for regulating PRMT functions.

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Section: Localization Of Prmt-gfp Fusion Proteins In Live Cellssupporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

Human protein arginine methyltransferases in vivo – distinct properties of eight canonical members of the PRMT family

Herrmann

Pably

Eckerich

et al. 2009

Journal of Cell Science

129

114

View full text Add to dashboard Cite

show abstract

“…Indeed, it interacts with the retinoblastoma gene product, which is an important regulator of the transcription factor E2F (18,45). Prmt2 can also directly regulate transcription factor activity like the estrogen receptor-a (45), Stat3 (46) and the androgen receptor (47). Moreover, Prmt2 directly modifies the structure of the chromatin, mediating an asymmetric methylation of histone H3(R8) after recruitment by b-catenin on its targeted genes, establishing a poised chromatin architecture necessary and sufficient to regulate expression of key organizer genes (48,49).…”

Section: Discussionmentioning

confidence: 99%

Prmt2 Regulates the Lipopolysaccharide-Induced Responses in Lungs and Macrophages

Dalloneau

Pereira

Brault

et al. 2011

The Journal of Immunology

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Precise control of the LPS stimulation in the lung modulates inflammation and airway hyperresponsiveness involving the well-known TLR4/NF-κB pathway. As a consequence, the expression and secretion of proinflammatory cytokines is tightly regulated with the recruitment of neutrophils. Changes in the LPS-induced responses have been observed in the Prmt2-Col6a1 monosomic model, suggesting the presence of dosage-sensitive genes controlling LPS pathway in the mouse. In this article, we report that the Prmt2 regulates the LPS-induced lung responses in lungs and macrophages. We demonstrate that Prmt2 gene dosage influences the lung airway hyperresponsiveness, the recruitment of neutrophils, and the expression of proinflammatory cytokines, such as IL-6 and TNF-α. In addition, Prmt2 loss of function also altered the nuclear accumulation of NF-κB in stimulated macrophages. Prmt2 should be considered as a new member of the NF-κB pathway controlling LPS-induced inflammatory and lung responses in a dosage-dependent manner, certainly through regulating nuclear accumulation of NF-κB as shown already in fibroblasts.

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“…PRMT2 has been recently identified as a type I enzyme (31). Both PRMT1 and PRMT2 can function as a coactivator in regulating gene expression (32)(33)(34)(35). In contrast to PRMT1, which suppressed differentiation, ectopic expression of PRMT2 had no apparent effect on PMA-induced differentiation (Fig.…”

Section: Human Cd34mentioning

confidence: 97%

Protein-arginine Methyltransferase 1 Suppresses Megakaryocytic Differentiation via Modulation of the p38 MAPK Pathway in K562 Cells

Chang¹,

Hua²,

Yao

et al. 2010

Journal of Biological Chemistry

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Protein-arginine methyltransferase 1 (PRMT1) plays pivotal roles in various cellular processes. However, its role in megakaryocytic differentiation has yet to be investigated. Human leukemia K562 cells have been used as a model to study hematopoietic differentiation. In this study, we report that ectopic expression of HA-PRMT1 in K562 cells suppressed phorbol 12-myristate 13-acetate (PMA)-induced megakaryocytic differentiation as demonstrated by changes in cytological characteristics, adhesive properties, and CD41 expression, whereas knockdown of PRMT1 by small interference RNA promoted differentiation. Impairment of the methyltransferase activity of PRMT1 diminished the suppressive effect. These results provide evidence for a novel role of PRMT1 in negative regulation of megakaryocytic differentiation. Activation of ERK MAPK has been shown to be essential for megakaryocytic differentiation, although the role of p38 MAPK is still poorly understood. We show that knockdown of p38␣ MAPK or treatment with the p38 inhibitor SB203580 significantly enhanced PMA-induced megakaryocytic differentiation. Further investigation revealed that PRMT1 promotes activation of p38 MAPK without inhibiting activation of ERK MAPK. In p38␣ knockdown cells, PRMT1 could no longer suppress differentiation. In contrast, enforced expression of p38␣ MAPK suppressed PMAinduced megakaryocytic differentiation of parental K562 as well as PRMT1-knockdown cells. We propose modulation of the p38 MAPK pathway by PRMT1 as a novel mechanism regulating megakaryocytic differentiation. This study thus provides a new perspective on the promotion of megakaryopoiesis.

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PRMT2, a member of the protein arginine methyltransferase family, is a coactivator of the androgen receptor

Cited by 82 publications

References 56 publications

Human protein arginine methyltransferases in vivo – distinct properties of eight canonical members of the PRMT family

Human protein arginine methyltransferases in vivo – distinct properties of eight canonical members of the PRMT family

Prmt2 Regulates the Lipopolysaccharide-Induced Responses in Lungs and Macrophages

Protein-arginine Methyltransferase 1 Suppresses Megakaryocytic Differentiation via Modulation of the p38 MAPK Pathway in K562 Cells

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