期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2005
卷号：102
期号：23
页码：8126-8131
DOI：10.1073/pnas.0503197102
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Mitogen-activated protein kinase-mediated growth factor signals are known to augment the ligand-induced transactivation function of nuclear estrogen receptor {alpha} (ER{alpha}) through phosphorylation of Ser-118 within the ER{alpha} N-terminal transactivation (activation function-1) domain. We identified the spliceosome component splicing factor (SF)3a p120 as a coactivator specific for human ER{alpha} (hER{alpha}) activation function-1 that physically associated with ER{alpha} dependent on the phosphorylation state of Ser-118. SF3a p120 potentiated hER{alpha}-mediated RNA splicing, and notably, the potentiation of RNA splicing by SF3a p120 depended on hER Ser-118 phosphorylation. Thus, our findings suggest a mechanism by which growth factor signaling can regulate gene expression through the modulation of RNA splicing efficiency via phosphorylation of sequence-specific activators, after association between such activators and the spliceosome.
