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RSRC1 SUMOylation enhances SUMOylation and inhibits transcriptional activity of estrogen receptor ß.
Chen, Lihan; Li, Weini; Qiu, Weiyi; Ren, Wen; Li, Qincao; Han, Baiyu; Zhou, Lei; Cheng, Long; Zhang, Hao; Ye, Qinong.
Afiliación
  • Chen L; Department of Medical Molecular Biology, Beijing Institute of Biotechnology, Beijing 100850, PR China.
  • Li W; Department of Medical Molecular Biology, Beijing Institute of Biotechnology, Beijing 100850, PR China.
  • Qiu W; Department of Medical Molecular Biology, Beijing Institute of Biotechnology, Beijing 100850, PR China.
  • Ren W; Department of Medical Molecular Biology, Beijing Institute of Biotechnology, Beijing 100850, PR China.
  • Li Q; Department of Medical Molecular Biology, Beijing Institute of Biotechnology, Beijing 100850, PR China.
  • Han B; Department of Medical Molecular Biology, Beijing Institute of Biotechnology, Beijing 100850, PR China.
  • Zhou L; Department of Medical Molecular Biology, Beijing Institute of Biotechnology, Beijing 100850, PR China.
  • Cheng L; Department of Medical Molecular Biology, Beijing Institute of Biotechnology, Beijing 100850, PR China. Electronic address: flonic@163.com.
  • Zhang H; Department of Medical Molecular Biology, Beijing Institute of Biotechnology, Beijing 100850, PR China; Cardiovascular Drug Research Center, Tianjin Institute of Health and Environmental Medicine, Tianjin 300050, PR China. Electronic address: zhanghal197@163.com.
  • Ye Q; Department of Medical Molecular Biology, Beijing Institute of Biotechnology, Beijing 100850, PR China. Electronic address: yeqn66@yahoo.com.
FEBS Lett ; 589(13): 1476-84, 2015 Jun 04.
Article en En | MEDLINE | ID: mdl-25937118
The transcription factor estrogen receptor ß (ERß) plays roles in the central nervous, endocrine, cardiovascular, and immune systems. ERß can be SUMOylated. However, the underlying mechanism remains unclear. Here, we show that RSRC1/SRrp53 interacts with ERß and SUMOylation of RSRC1 is required for regulation of PIAS1-mediated ERß SUMOylation. RSRC1 promotes ERß SUMOylation through enhanced interaction between ERß and PIAS1. RSRC1 represses ERß transcriptional activity through regulation of ERß SUMOylation. By establishing RSRC1 as a novel cofactor for SUMOylation, our data provide insight into regulation of ERß SUMOylation and indicate that SUMOylation of one protein can regulate another protein SUMOylation.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transcripción Genética / Proteínas Nucleares / Receptor beta de Estrógeno / Sumoilación Límite: Humans Idioma: En Revista: FEBS Lett Año: 2015 Tipo del documento: Article Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transcripción Genética / Proteínas Nucleares / Receptor beta de Estrógeno / Sumoilación Límite: Humans Idioma: En Revista: FEBS Lett Año: 2015 Tipo del documento: Article Pais de publicación: Reino Unido