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Glucocorticoid receptor phosphorylation: overview, function and cell cycle-dependence

J E Bodwell1, J C Webster, C M Jewell

  • 1Department of Physiology, Dartmouth Medical School, Lebanon, NH 03756, USA.

The Journal of Steroid Biochemistry and Molecular Biology
|August 12, 1998
PubMed
Summary
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Steroid hormone receptor phosphorylation, particularly hyperphosphorylation, subtly modulates receptor function rather than acting as an on-off switch. This process is cell cycle-dependent, impacting receptor activity and stability.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Endocrinology

Background:

  • Steroid hormone receptors are known to be phosphorylated, with hormone-induced hyperphosphorylation occurring in most cases.
  • Phosphorylation sites are predominantly serines in the N-terminal domain, but other residues and domains can also be modified.

Purpose of the Study:

  • To investigate the role and regulation of steroid hormone receptor phosphorylation, focusing on hormone-induced hyperphosphorylation.
  • To explore the functional consequences of altered phosphorylation, including its relationship with the cell cycle.

Main Methods:

  • Analysis of phosphorylated residues and domains in various steroid hormone receptors.
  • Site-directed mutagenesis (e.g., alanine substitutions) to assess the impact of phosphorylation.

Related Experiment Videos

  • Cell cycle analysis to correlate phosphorylation patterns with receptor activity.

    • Main Results:

    • Hyperphosphorylation is not a simple on-off switch but a modulator of receptor function, with mutations decreasing activity by up to 90%.
    • Glucocorticoid receptor hyperphosphorylation is specific to agonists, follows activation, and does not create new sites, unlike some other receptors.
    • Both basal and hormone-dependent phosphorylation are cell cycle-dependent, influencing glucocorticoid receptor activity, repression, and protein stability.

    Conclusions:

    • Steroid hormone receptor phosphorylation plays a subtle, modulatory role in receptor function, influenced by agonists, antagonists, and the cell cycle.
    • The N-terminal domain's negative charge, regulated by basal phosphorylation, controls hyperphosphorylation and is linked to cell cycle-dependent glucocorticoid activity.