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Vol. 16, Issue 1, 231-237, January 2005
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Membrane Localization: Regulation by 17
-Estradiol
* Department of Biology, University Roma Tre, I-00146 Rome, Italy;
Interdepartmental Laboratory for Electron Microscopy, University Roma Tre, I-00146 Rome, Italy;
National Institute for Infectious Diseases Istituto di Ricovero e Cura a Carattere Scientifico Lazzaro Spallanzani, I-00149 Rome, Italy;
Department of Chemistry, Chemical Engineering, and Materials, University of L'Aquila, I-67100 L'Aquila, Italy; and
|| Department of Experimental Biology, University of Bologna, I-40126 Bologna, Italy
Submitted July 2, 2004;
Revised September 28, 2004;
Accepted October 4, 2004
Monitoring Editor: Keith Yamamoto
A fraction of the nuclear estrogen receptor 
(ER) is localized to the plasma membrane region of 17
-estradiol (E2) target cells. We previously reported that ER is a palmitoylated protein. To gain insight into the molecular mechanism of ER residence at the plasma membrane, we tested both the role of palmitoylation and the impact of E2 stimulation on ER membrane localization. The cancer cell lines expressing transfected or endogenous human ER (HeLa and HepG2, respectively) or the ER nonpalmitoylable Cys447Ala mutant transfected in HeLa cells were used as experimental models. We found that palmitoylation of ER enacts ER association with the plasma membrane, interaction with the membrane protein caveolin-1, and nongenomic activities, including activation of signaling pathways and cell proliferation (i.e., ERK and AKT activation, cyclin D1 promoter activity, DNA synthesis). Moreover, E2 reduces both ER palmitoylation and its interaction with caveolin-1, in a time- and dose-dependent manner. These data point to the physiological role of ER palmitoylation in the receptor localization to the cell membrane and in the regulation of the E2-induced cell proliferation.
Abbreviations used: 2-Br, 2-bromohexadecanoic acid, 2-bromopalmitate; E2, 17-estradiol; ER, estrogen receptor; ERK, extracellular signal-regulated kinase; IGF-1, insulin-like growth factor-1; PAT, palmitoyl acyl transferase; PI3K, phosphoinositide-3-kinase.
¶ Corresponding author. E-mail address: m.marino{at}uniroma3.it.
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