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PMID:12039952

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Citation

Qi, C, Chang, J, Zhu, Y, Yeldandi, AV, Rao, SM and Zhu, YJ (2002) Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha. J. Biol. Chem. 277:28624-30

Abstract

In an attempt to isolate cofactors capable of influencing estrogen receptor alpha (ERalpha) transcriptional activity, we used yeast two-hybrid screening and identified protein arginine methyltransferase 2 (PRMT2) as a new ERalpha-binding protein. PRMT2 interacted directly with three ERalpha regions including AF-1, DNA binding domain, and hormone binding domain in a ligand-independent fashion. The ERalpha-interacting region on PRMT2 has been mapped to a region encompassing amino acids 133-275. PRMT2 also binds to ERbeta, PR, TRbeta, RARalpha, PPARgamma, and RXRalpha in a ligand-independent manner. PRMT2 enhanced both ERalpha AF-1 and AF-2 transcriptional activity, and the potential methyltransferase activity of PRMT2 appeared pivotal for its coactivator function. In addition, PRMT2 enhanced PR, PPARgamma, and RARalpha-mediated transactivation. Although PRMT2 was found to interact with two other coactivators, the steroid receptor coactivator-1 (SRC-1) and the peroxisome proliferator-activated receptor-interacting protein (PRIP), no synergistic enhancement of ERalpha transcriptional activity was observed when PRMT2 was coexpressed with either PRIP or SRC-1. In this respect PRMT2 differs from coactivators PRMT1 and CARM1 (coactivator-associated arginine methyltransferase). These results suggest that PRMT2 is a novel ERalpha coactivator.

Links

PubMed Online version:10.1074/jbc.M201053200

Keywords

Animals; COS Cells; Cells, Cultured; DNA/metabolism; DNA, Complementary/metabolism; Dimerization; Estrogen Receptor alpha; Gene Library; Glutathione Transferase/metabolism; Humans; Plasmids/metabolism; Protein Binding; Protein Structure, Tertiary; Protein-Arginine N-Methyltransferases/metabolism; Protein-Arginine N-Methyltransferases/physiology; Receptors, Cytoplasmic and Nuclear/metabolism; Receptors, Estrogen/metabolism; Receptors, Retinoic Acid/metabolism; Transcription Factors/metabolism; Transcription, Genetic; Transcriptional Activation; Transfection; Two-Hybrid System Techniques; beta-Galactosidase/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:ESR1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P55345

F

Seeded From UniProt

complete

HUMAN:PRGR

enables

GO:0019899: enzyme binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P55345

F

Seeded From UniProt

complete

HUMAN:RARA

enables

GO:0019899: enzyme binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P55345

F

Seeded From UniProt

complete

HUMAN:RXRA

enables

GO:0019899: enzyme binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P55345

F

Seeded From UniProt

complete

HUMAN:ANM2

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q14686

F

Seeded From UniProt

complete

HUMAN:ANM2

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q15788

F

Seeded From UniProt

complete

HUMAN:ANM2

enables

GO:0033142: progesterone receptor binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P06401

F

Seeded From UniProt

complete

HUMAN:ANM2

enables

GO:0030331: estrogen receptor binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P03372

F

Seeded From UniProt

complete

HUMAN:ANM2

enables

GO:0030331: estrogen receptor binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q92731

F

Seeded From UniProt

complete

HUMAN:ANM2

enables

GO:0042803: protein homodimerization activity

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P55345

F

Seeded From UniProt

complete

HUMAN:ANM2

enables

GO:0042974: retinoic acid receptor binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P10276

F

Seeded From UniProt

complete

HUMAN:ANM2

enables

GO:0042974: retinoic acid receptor binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P19793

F

Seeded From UniProt

complete

HUMAN:ANM2

enables

GO:0042975: peroxisome proliferator activated receptor binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P37231

F

Seeded From UniProt

complete

HUMAN:ANM2

involved_in

GO:0045893: positive regulation of transcription, DNA-templated

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:ANM2

enables

GO:0046966: thyroid hormone receptor binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P10828

F

Seeded From UniProt

complete

HUMAN:ANM2

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P03372

F

Seeded From UniProt

complete

HUMAN:ANM2

enables

GO:0003713: transcription coactivator activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:NCOA6

enables

GO:0019899: enzyme binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P55345

F

Seeded From UniProt

complete

HUMAN:NCOA1

enables

GO:0019899: enzyme binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P55345

F

Seeded From UniProt

complete

HUMAN:ESR2

enables

GO:0019899: enzyme binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P55345

F

Seeded From UniProt

complete

HUMAN:ESR1

enables

GO:0019899: enzyme binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P55345

F

Seeded From UniProt

complete

HUMAN:THB

enables

GO:0019899: enzyme binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P55345

F

Seeded From UniProt

complete

HUMAN:PPARG

enables

GO:0019899: enzyme binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P55345

F

Seeded From UniProt

complete


See also

References

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