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Mol. Cells 2008; 25(2): 289-293

Published online April 30, 2008

© The Korean Society for Molecular and Cellular Biology

Repression of Transcriptional Activity of Estrogen Receptor alpha by a Cullin3/SPOP Ubiquitin E3 Ligase Complex

Boohyeong Byun and Yunhwa Jung

Abstract

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.

Keywords Cullin3-based E3 Ubiquitin Ligase Complex, ER alpha, SPOP, Ubiquitination

Article

Communication

Mol. Cells 2008; 25(2): 289-293

Published online April 30, 2008

Copyright © The Korean Society for Molecular and Cellular Biology.

Repression of Transcriptional Activity of Estrogen Receptor alpha by a Cullin3/SPOP Ubiquitin E3 Ligase Complex

Boohyeong Byun and Yunhwa Jung

Abstract

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.

Keywords: Cullin3-based E3 Ubiquitin Ligase Complex, ER alpha, SPOP, Ubiquitination

Mol. Cells
Aug 31, 2022 Vol.45 No.8, pp. 513~602
COVER PICTURE
Cryo-EM structure of human porphyrin transporter ABCB6 (main figure) shows that binding of hemin (inset, magenta) in concert with two glutathione molecules (cyan) primes ABCB6 for high ATP turnover (Kim et al., pp. 575-587).

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