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Department of Biology, University ‘Roma Tre’, Viale G Marconi, 446,I-00146 Roma, Italy

(Requests for offprints should be addressed to M Marino; Email: m.marino{at}uniroma3.it)

The cellular functions regulated by 17ß-estradiol (E2) start after the hormone binds to its receptors (i.e., ER and ERß ). These act as ligand-dependent transcription factor transactivating target genes. In addition, E2 induces non-genomic actions, whose activation is triggered by a fraction of the ERs localized at the plasma membrane. Palmitoylation allows ER to localize at the plasma membrane, to associate with caveolin-1, and, upon E2 stimulation, to activate rapid signals relevant for cell proliferation. The existence of a mechanism, which allows ERß localization at the plasma membrane and its putative role in anti-proliferative E2 effects is completely unknown. Here, the susceptibility of ERß to undergo palmitoylation and the role played by this process has been analyzed in DLD-1 containing endogenous ERß or in HeLa cells transiently transfected with ERß or ER expression vectors. As for ER , palmitoylation is necessary for ERß localization at the plasma membrane and its association with caveolin-1 but, in contrast to ER , the E2 binding increases ERß association with caveolin-1 and the p38 member of MAPK family. Moreover, the palmitoyl acyl transferase (PAT) inhibitor blocks the ability of ERß –E2 complex to activate p38 impairing the receptor-dependent activation of downstream proapoptotic cascade (i.e., caspase-3 activation and poly(ADP-ribose)polymerase (PARP) cleavage). Consequently, palmitoylation must be considered to be a molecular device for ERß , which allows these receptors to interact with the plasma membrane and to regulate E2-induced non-genomic functions relevant to the anti-proliferative effect of this hormone.

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