2002
DOI: 10.1074/jbc.m201053200
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Identification of Protein Arginine Methyltransferase 2 as a Coactivator for Estrogen Receptor α

Abstract: In an attempt to isolate cofactors capable of influencing estrogen receptor ␣ (ER␣) transcriptional activity, we used yeast two-hybrid screening and identified protein arginine methyltransferase 2 (PRMT2) as a new ER␣-binding protein. PRMT2 interacted directly with three ER␣ regions including AF-1, DNA binding domain, and hormone binding domain in a ligand-independent fashion. The ER␣-interacting region on PRMT2 has been mapped to a region encompassing amino acids 133-275. PRMT2 also binds to ER␤, PR, TR␤, RAR… Show more

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Cited by 149 publications
(126 citation statements)
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“…GST pull-down assays were performed using GST-Acinus-SЈ C terminus and in vitro-transcribed and -translated [ VOL. 28,2008 Acinus-SЈ IS A MODULATOR OF RAR ACTIVITY 2555 components of basal transcriptional machinery and general coactivators and corepressors, N-terminal A/B domains can interact with proteins involved in processes such as mRNA processing and splicing (p68, SRA, ANT-1, and p54nrb), with chaperones (BAG-1) or with a number of proteins containing specific enzymatic activities such as acetyl-and methyltransferases (12,17,25,34,39,43).…”
Section: Discussionmentioning
confidence: 99%
“…GST pull-down assays were performed using GST-Acinus-SЈ C terminus and in vitro-transcribed and -translated [ VOL. 28,2008 Acinus-SЈ IS A MODULATOR OF RAR ACTIVITY 2555 components of basal transcriptional machinery and general coactivators and corepressors, N-terminal A/B domains can interact with proteins involved in processes such as mRNA processing and splicing (p68, SRA, ANT-1, and p54nrb), with chaperones (BAG-1) or with a number of proteins containing specific enzymatic activities such as acetyl-and methyltransferases (12,17,25,34,39,43).…”
Section: Discussionmentioning
confidence: 99%
“…Although the methyltransferase activity of PRMT2 has not been demonstrated, PRMT2 has been implicated in transcriptional regulation in vivo. PRMT2 is unable to stimulate transcription as a Gal4-PRMT2 fusion, but it is able to bind a number of hormone receptors including ERa, ERb, PR, TRb, and RARa in a ligand independent manner and coactivate transcription (Qi et al, 2002). In contrast, PRMT2 can also interact with RB and repress the transcriptional activity of E2F1 by forming a ternary complex with E2F1 through RB .…”
Section: Protein Arginine Methyltransferasesmentioning
confidence: 99%
“…Plasmids and Antibodies-pCDNA3.1-ER␣, ERE-TK-LUC, and glutathione S-transferase (GST)-ER␣ (LBD) were described as before (28). set was constructed by inserting the C-terminal 172-aminoacid coding region of mouse MLL2 into the EcoRI/XhoI site of pGEX-5X-1 vector (Amersham Biosciences).…”
Section: Methodsmentioning
confidence: 99%