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MBC in Press, published online ahead of print October 20, 2004
Mol. Biol. Cell 10.1091/mbc.E04-07-0547

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Submitted on July 2, 2004
Revised on September 28, 2004
Accepted on October 4, 2004

Palmitoylation-dependent Estrogen Receptor {alpha} Membrane Localization: Regulation by 17{beta}-Estradiol

Filippo Acconcia,* Paolo Ascenzi,*{dagger}{ddagger} Alessio Bocedi,{ddagger}{sect} Enzo Spisni,|| Vittorio Tomasi,|| Anna Trentalance,* Paolo Visca,*{ddagger} and Maria Marino*¶

*Department of Biology, University Roma Tre, I-00146 Rome, Italy; {dagger}Interdepartmental Laboratory for Electron Microscopy, University Roma Tre, I-00146 Rome, Italy; {ddagger}National Institute for Infectious Diseases Istituto di Ricovero e Cura a Carattere Scientifico Lazzaro Spallanzani, I-00149 Rome, Italy; {sect}Department of Chemistry, Chemical Engineering, and Materials, University of L’Aquila, I-67100 L’Aquila, Italy; ||Department of Experimental Biology, University of Bologna, I-40126 Bologna, Italy

Monitoring Editor: Keith Yamamoto

A fraction of the nuclear estrogen receptor {alpha} (ER{alpha}) is localized to the plasma membrane region of 17{beta}-estradiol (E2) target cells. We previously reported that ER{alpha} is a palmitoylated protein. To gain insight into the molecular mechanism of ER{alpha} residence at the plasma membrane we tested both the role of palmitoylation and the impact of E2 stimulation on ER{alpha} membrane localization. The cancer cell lines expressing transfected or endogenous human ER{alpha} (HeLa and HepG2, respectively) or the ER{alpha} nonpalmitoylable Cys447Ala mutant transfected in HeLa cells were used as experimental models. We found that palmitoylation of ER{alpha} enacts ER{alpha} 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{alpha} palmitoylation and its interaction with caveolin-1, in a time- and dose-dependent manner. These data point to the physiological role of ER{alpha} palmitoylation in the receptor localization to the cell membrane and in the regulation of the E2-induced cell proliferation.

Corresponding author. E-mail: m.marino{at}uniroma3.it






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