Title : Phosphorylation of serine 212 confers novel activity to human estrogen receptor α.

Pub. Date : 2012 Apr

PMID : 22266331






9 Functional Relationships(s)
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1 Phosphorylation of serine 212 confers novel activity to human estrogen receptor alpha. Serine estrogen receptor 1 Homo sapiens
2 Estrogen receptor alpha (ERalpha) can be phosphorylated at various residues, one of which is serine 212 in the DNA binding domain. Serine estrogen receptor 1 Homo sapiens
3 Estrogen receptor alpha (ERalpha) can be phosphorylated at various residues, one of which is serine 212 in the DNA binding domain. Serine estrogen receptor 1 Homo sapiens
4 Here, we have investigated the role of phosphorylated serine 212 in the regulation of ERalpha activity by comparing it with serine 236, another potential phosphorylation site within the DNA binding domain, and demonstrated that phosphorylation of serine 212 confers upon ERalpha a distinct activity regulating gene expression in Huh-7 cells. Serine estrogen receptor 1 Homo sapiens
5 Here, we have investigated the role of phosphorylated serine 212 in the regulation of ERalpha activity by comparing it with serine 236, another potential phosphorylation site within the DNA binding domain, and demonstrated that phosphorylation of serine 212 confers upon ERalpha a distinct activity regulating gene expression in Huh-7 cells. Serine estrogen receptor 1 Homo sapiens
6 Here, we have investigated the role of phosphorylated serine 212 in the regulation of ERalpha activity by comparing it with serine 236, another potential phosphorylation site within the DNA binding domain, and demonstrated that phosphorylation of serine 212 confers upon ERalpha a distinct activity regulating gene expression in Huh-7 cells. Serine estrogen receptor 1 Homo sapiens
7 cDNA microarray and Ingenuity Pathway Analysis, employed on Huh-7 cells ectopically expressing either ERalpha S212A or ERalpha S212D, revealed that phosphorylation of serine 212 enabled ERalpha to regulate a unique set of genes and cellular functions. Serine estrogen receptor 1 Homo sapiens
8 cDNA microarray and Ingenuity Pathway Analysis, employed on Huh-7 cells ectopically expressing either ERalpha S212A or ERalpha S212D, revealed that phosphorylation of serine 212 enabled ERalpha to regulate a unique set of genes and cellular functions. Serine estrogen receptor 1 Homo sapiens
9 cDNA microarray and Ingenuity Pathway Analysis, employed on Huh-7 cells ectopically expressing either ERalpha S212A or ERalpha S212D, revealed that phosphorylation of serine 212 enabled ERalpha to regulate a unique set of genes and cellular functions. Serine estrogen receptor 1 Homo sapiens