Estrogen Receptor Phosphorylation

Steroids. 2003 Jan;68(1):1-9. doi: 10.1016/s0039-128x(02)00110-1.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Estrogen Receptor alpha
  • Humans
  • MAP Kinase Signaling System
  • Phosphorylation
  • Receptor Cross-Talk
  • Receptors, Estrogen / metabolism*
  • Receptors, Estrogen / physiology

Substances

  • Estrogen Receptor alpha
  • Receptors, Estrogen
  • Cyclic AMP-Dependent Protein Kinases