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Related Experiment Videos

Glucocorticoid receptor phosphorylation, transformation, and DNA binding.

W Tienrungroj1, E R Sanchez, P R Housley

  • 1Department of Pharmacology, University of Michigan Medical School, Ann Arbor 48109.

The Journal of Biological Chemistry
|December 25, 1987
PubMed
Summary

Glucocorticoid receptor (GR) phosphorylation remains unchanged during temperature-induced transformation to a DNA-binding state. Both bound and unbound GR are equally phosphorylated, indicating phosphorylation does not regulate GR-DNA binding.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Glucocorticoid receptors (GR) mediate cellular responses to glucocorticoids.
  • Receptor transformation to a DNA-binding state is a key regulatory step.
  • The role of GR phosphorylation in this process is not fully understood.

Purpose of the Study:

  • To investigate the phosphorylation state of the glucocorticoid receptor before and after transformation to its DNA-binding state.
  • To determine if phosphorylation influences GR binding to DNA.

Main Methods:

  • Immunoadsorption of GR from L cell cytosol using [32P]orthophosphate labeling.
  • Temperature-mediated transformation of GR under cell-free conditions.
  • Incubation of cytosol with DNA-cellulose to assess DNA binding.

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  • Analysis of nuclear translocation in intact cells upon hormone treatment.
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting.

    • Main Results:

    • Temperature-induced transformation of GR in cell-free systems did not alter receptor size or phosphorylation degree.
    • Both DNA-bound and unbound GR fractions showed similar phosphorylation levels.
    • In intact cells, hormone-induced nuclear translocation of GR was temperature and ligand-dependent.
    • Nuclear-bound and cytosolic GR were phosphorylated to comparable extents.

    Conclusions:

    • Glucocorticoid receptor phosphorylation does not appear to be a critical factor in the transformation to a DNA-binding state or in DNA binding itself.
    • The transformation process and subsequent nuclear translocation are regulated by temperature and ligand binding, not by changes in phosphorylation status.