RSRC1 SUMOylation enhances SUMOylation and inhibits transcriptional activity of estrogen receptor β. Issue 13 (30th April 2015)

• Record Type: Journal Article
• Authors: Chen, Lihan; Li, Weini; Qiu, Weiyi; Ren, Wen; Li, Qincao; Han, Baiyu; Zhou, Lei; Cheng, Long; Zhang, Hao; Ye, Qinong
• Is Part Of: FEBS letters. Volume 589:Issue 13(2015)
• Page Start: 1476
• Page End: 1484
• Publication Date: 2015-04-30
• Subjects: SUMOylation -- Transcriptional activity -- ERβ -- RSRC1/SRrp53 -- PIAS1; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2015.04.035
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : The transcription factor estrogen receptor β (ERβ) plays roles in the central nervous, endocrine, cardiovascular, and immune systems. ERβ can be SUMOylated. However, the underlying mechanism remains unclear. Here, we show that RSRC1/SRrp53 interacts with ERβ and SUMOylation of RSRC1 is required for regulation of PIAS1‐mediated ERβ SUMOylation. RSRC1 promotes ERβ SUMOylation through enhanced interaction between ERβ and PIAS1. RSRC1 represses ERβ transcriptional activity through regulation of ERβ SUMOylation. By establishing RSRC1 as a novel cofactor for SUMOylation, our data provide insight into regulation of ERβ SUMOylation and indicate that SUMOylation of one protein can regulate another protein SUMOylation. Abstract : RSRC1 interacts with ERβ. RSRC1 SUMOylation enhances PIAS1‐mediated ERβ SUMOylation. RSRC1 promotes ERβ SUMOylation through enhanced ERβ/PIAS1 interaction. RSRC1 represses ERβ transcriptional activity via ERβ SUMOylation.