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Steroids. 2003 Jan;68(1):1-9.

Estrogen receptor phosphorylation.

Author information

1
Center for Cell Signaling, Health Sciences Center, University of Virginia, Hospital West, Room 7041, Box 800577, Charlottesville, VA 22908-0577, USA. dal5f@virginia.edu

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.

PMID:
12475718
DOI:
10.1016/s0039-128x(02)00110-1
[Indexed for MEDLINE]

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