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棕榈酰化作用是否会将雌激素受体靶向至质膜小窝?

Does palmitoylation target estrogen receptors to plasma membrane caveolae?

作者信息

Acconcia Filippo, Bocedi Alessio, Ascenzi Paolo, Marino Maria

机构信息

Dipartimento di Biologia, Università Roma Tre, Viale Guglielmo Marconi 446, I-00146, Roma, Italy.

出版信息

IUBMB Life. 2003 Jan;55(1):33-5. doi: 10.1080/1521654031000081256.

Abstract

The human nuclear estrogen receptors (i.e., ERalpha and ERbeta), as other transcriptional factors, regulate cellular processes inducing genomic events. In addition, the binding of 17beta-estradiol to ERs induces different membrane initiating non-genomic signaling. The non-genomic effects of ER are independent of transcriptional activity of the receptor and have been attributed to membrane ERs belonging to a signaling complex localized in caveolae. Here, we postulate that S-acylation of cysteine residue(s) present in the ligand binding domain of ERalpha and ERbeta may play a critical role in the membrane caveolar localization of the receptor and in the formation of the 'steroid signalosome'.

摘要

人类核雌激素受体(即雌激素受体α和雌激素受体β)与其他转录因子一样,通过诱导基因组事件来调节细胞过程。此外,17β-雌二醇与雌激素受体的结合会引发不同的膜起始非基因组信号传导。雌激素受体的非基因组效应独立于受体的转录活性,并且被认为归因于位于小窝中的信号复合物中的膜雌激素受体。在此,我们推测雌激素受体α和雌激素受体β配体结合域中存在的半胱氨酸残基的S-酰化可能在受体的膜小窝定位以及“类固醇信号体”的形成中起关键作用。

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