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in SK-N-BE Neuroblastoma and COS-1 Renal Carcinoma Cells
Centre Molecular Pharmacology Laboratory (C.P., S.S., P.A., A.M.) and Atherosclerosis Laboratory (E.G.) Institute of Pharmacological Sciences University of Milan Milan, Italy 1–20133
The 
-estrogen receptor (ER) transcriptional
activity can be regulated either by binding to the cognate ligand or by
intracellular signaling pathways responsive to a variety of factors
acting through cell membrane receptors. Studies carried out in HeLa and
COS-1 cells demonstrated that the cross-coupling between estrogen and
growth factor receptors is mediated by p21ras and requires
phosphorylation of a specific serine residue (Ser 118 in the human
ER and Ser 122 in mouse ER) located in the ER N-terminal
activation function 1 (AF-1). Likewise, in the SK-N-BE neuroblastoma
cell line p21ras is involved in the cross-coupling between
insulin and ER receptors. However, in this cell line Ser 122 is not
necessary for insulin-dependent activation of unliganded ER. In
addition, after insulin activation, the electrophoretic mobility
associated to serine hyperphosphorylation of ER in SK-N-BE and in
COS-1 cells is different. Our study rules out the possibility of
tyrosine phosporylation in unliganded ER activation by means of
transactivation studies of ER tyrosine mutants and analysis of Tyr
phosphorylation immunoreactivity. The two cofactors for steroid
receptors RIP 140 and SRC-1 do not seem to be specifically involved in
the insulin-induced ER transactivation. The present study
demonstrates the possibility of an alternative, cell-specific pathway
of cross-coupling between intracellular and membrane receptors, which
might be of importance for the understanding of the physiological
significance of this mode of activation in the nervous system.
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