PubMed:12039952
Annnotations
sentences
{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":100},"obj":"Sentence"},{"id":"T2","span":{"begin":101,"end":347},"obj":"Sentence"},{"id":"T3","span":{"begin":348,"end":496},"obj":"Sentence"},{"id":"T4","span":{"begin":497,"end":598},"obj":"Sentence"},{"id":"T5","span":{"begin":599,"end":704},"obj":"Sentence"},{"id":"T6","span":{"begin":705,"end":873},"obj":"Sentence"},{"id":"T7","span":{"begin":874,"end":955},"obj":"Sentence"},{"id":"T8","span":{"begin":956,"end":1273},"obj":"Sentence"},{"id":"T9","span":{"begin":1274,"end":1390},"obj":"Sentence"},{"id":"T10","span":{"begin":1391,"end":1455},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha.\nIn 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."}
relna
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