Repression of transcriptional activity of estrogen receptor alpha by a Cullin3/SPOP ubiquitin E3 ligase complex.
The role of SPOP in the ubiquitination of ER alpha by the Cullin3-based E3 ubiquitin ligase complex was investigated. We showed that the N-terminal region of SPOP containing the MATH domain interacts with the AF-2 domain of ER alpha in cultured human embryonic 293 cells. SPOP was required for coimmunoprecipitation of ER alpha; with Cullin3. This is the first report of the essential role of SPOP in ERalpha ubiquitination by the Cullin3-based E3 ubiquitin ligase complex. We also demonstrated repression of the transactivation capability of ER alpha; in cultured mammalian cells.
Byun
Boohyeong
B
Department of Oriental Medicine, Daegu Haany University, Daegu 705-060, Korea. bhbyun@dhu.ac.kr
Jung
Yunhwa
Y
D002460:Cell Line; D044842:Cullin Proteins / Q000378:metabolism*; D047628:Estrogen Receptor alpha / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D011485:Protein Binding; D012097:Repressor Proteins / Q000378:metabolism*; D014158:Transcription, Genetic; D015533:Transcriptional Activation / Q000235:genetics; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D054875:Ubiquitination
D044842:Cullin Proteins; C506487:ESR1 protein, human; D047628:Estrogen Receptor alpha; D012097:Repressor Proteins; D044767:Ubiquitin-Protein Ligases