title: Estrogen receptor phosphorylation.
abstract: Estrogen receptor alpha (ERalpha) is phosphorylated on multiple amino acid residues. For example, in response to estradiol binding, human ERalpha is predominately phosphorylated on Ser-118 and to a lesser extent on Ser-104 and Ser-106. In response to activation of the mitogen-activated protein kinase pathway, phosphorylation occurs on Ser-118 and Ser-167. These serine residues are all located within the activation function 1 region of the N-terminal domain of ERalpha. In contrast, activation of protein kinase A increases the phosphorylation of Ser-236, which is located in the DNA-binding domain. The in vivo phosphorylation status of Tyr-537, located in the ligand-binding domain, remains controversial. In this review, I present evidence that these phosphorylations occur, and identify the kinases thought to be responsible. Additionally, the functional importance of ERalpha phosphorylation is discussed.
authors.affiliation: Center for Cell Signaling, Health Sciences Center, University of Virginia, Hospital West, Room 7041, Box 800577, Charlottesville, VA 22908-0577, USA. dal5f@virginia.edu
authors.forename: Deborah A
authors.initials: DA
authors.lastname: Lannigan
mesh_terms: D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D047628:Estrogen Receptor alpha; D006801:Humans; D020935:MAP Kinase Signaling System; D010766:Phosphorylation; D020239:Receptor Cross-Talk; D011960:Receptors, Estrogen / Q000378:metabolism* / Q000502:physiology
chemical_list: D047628:Estrogen Receptor alpha; D011960:Receptors, Estrogen; D017868:Cyclic AMP-Dependent Protein Kinases