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Proline-Directed Androgen Receptor Phosphorylation.

Yanfei Gao1, Shaoyong Chen1

  • 1Division of Hematology/Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School 330 Brookline, MA 02115, USA.

Journal of Molecular and Genetic Medicine : an International Journal of Biomedical Research
|April 14, 2015
PubMed
Summary
This summary is machine-generated.

Androgen receptor (AR) phosphorylation, especially proline-directed serine/threonine modifications in the N-terminal domain, significantly impacts its function. Targeting AR phosphorylation may enhance the effectiveness of antiandrogen therapies.

Keywords:
Androgen receptorKinasesPhosphatasePhosphorylationProline-directed serine/threonine phosphorylation

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Area of Science:

  • Molecular Biology
  • Endocrinology
  • Biochemistry

Background:

  • The androgen receptor (AR) is a crucial mediator of steroid hormone functions.
  • Post-translational modifications significantly regulate the activity of biological molecules like AR.

Purpose of the Study:

  • To review the reported activities and significance of AR phosphorylation.
  • To emphasize proline-directed serine/threonine phosphorylation on the AR.
  • To explore the therapeutic potential of targeting AR phosphorylation.

Main Methods:

  • Literature review of studies on AR phosphorylation.
  • Analysis of phosphorylation sites, particularly in the N-terminal domain.
  • Discussion of the interplay between AR phosphorylation and antiandrogen therapies.

Main Results:

  • AR functional activities are modulated by post-translational modifications, including phosphorylation.
  • Proline-directed serine/threonine phosphorylation is a predominant modification on the AR.
  • AR phosphorylation is highly enriched in the N-terminal domain.

Conclusions:

  • Targeting AR phosphorylation, particularly in the N-terminal domain, is a promising strategy.
  • Modulating AR phosphorylation may offer synergistic effects when combined with clinical antiandrogens targeting the C-terminal domain.