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Estrogen receptor phosphorylation

Steroids, ISSN: 0039-128X, Vol: 68, Issue: 1, Page: 1-9
2003
  • 403
    Citations
  • 0
    Usage
  • 213
    Captures
  • 2
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    403
  • Captures
    213
  • Mentions
    2
    • References
      2
      • 2

Review Description

Estrogen receptor α (ERα) is phosphorylated on multiple amino acid residues. For example, in response to estradiol binding, human ERα 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 ERα. 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 ERα phosphorylation is discussed.

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