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

Abstract excerpt

Estrogen receptor α (ERα) can be phosphorylated at various residues, one of which is serine 212 in the DNA binding domain. The majority of human nuclear receptors conserves, as a motif, this serine residue within their DNA binding domain. Among these nuclear receptors, phosphorylation of the corresponding threonine 38 in the nuclear receptor CAR is essential for determining its activity [9]. Here, we have...

Topics

• Amino Acid Sequence
• Binding Sites
• Blotting, Western
• Cell Line, Tumor
• Estrogen Receptor alpha
• Gene Expression Profiling
• Gene Expression Regulation, Neoplastic
• Humans
• Molecular Sequence Data
• Mutation
• Oligonucleotide Array Sequence Analysis
• Phosphorylation
• Reverse Transcriptase Polymerase Chain Reaction