Membrane association of estrogen receptor α and β influences 17β-estradiol-mediated cancer cell proliferation
- 作者：Maria Marino ; Paolo Ascenzi
- 关键词：Estrogen receptor
//www.sciencedirect.com/scidirimg/entities/204e.gif" alt="greek small letter alpha" title="greek small letter alpha" border="0"> ; Estrogen receptor β ; Estrogen receptor palmitoylation ; 17β ; -Estradiol ; Rapid sign
- 刊名：Steroids
- 出版年：2008
- 期刊代码：142_0039128x
- 类别：bio
- 出版时间：October 2008
- 卷：73
- 期：9-10
- 页码：853-858
- 文件大小：331 K
摘要
S-Palmitoylation is a widespread post-translational modification of integral and/or peripheral proteins occurring in all eukaryotic cells. The family of S-palmitoylated proteins is large and diverse and recently, estrogen receptor isoforms (ER
and ERβ) belonging to the nuclear receptor superfamily have been added to the palmitoylproteoma. S-Palmitoylation allows ER and ERβ localization at the plasma membrane, where they associate with caveolin-1. Upon 17β-estradiol (E2) stimulation, ER dissociates from caveolin-1 allowing the activation of rapid signals relevant for cell proliferation. In contrast to ER, E2 increases ERβ association with caveolin-1 and activates p38 kinase and the downstream pro-apoptotic cascade (i.e., caspase-3 activation and PARP cleavage). These data highlight the physiological role of palmitoylation in modulating the ER and ERβ localization at the plasma membrane and the regulation of different E2-induced non-genomic functions relevant for controlling cell proliferation.
and ERβ) belonging to the nuclear receptor superfamily have been added to the palmitoylproteoma. S-Palmitoylation allows ER and ERβ localization at the plasma membrane, where they associate with caveolin-1. Upon 17β-estradiol (E2) stimulation, ER dissociates from caveolin-1 allowing the activation of rapid signals relevant for cell proliferation. In contrast to ER, E2 increases ERβ association with caveolin-1 and activates p38 kinase and the downstream pro-apoptotic cascade (i.e., caspase-3 activation and PARP cleavage). These data highlight the physiological role of palmitoylation in modulating the ER and ERβ localization at the plasma membrane and the regulation of different E2-induced non-genomic functions relevant for controlling cell proliferation.