Glucocorticoid receptor phosphorylation in mouse L-cells

Edwin R. Sanchez*, Wilai Tienrungroj, Friedrich C. Dalman, Alexander L Y Lin

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


This paper summarizes our observations on the phosphorylation state of untransformed and transformed glucocorticoid receptors isolated from 32P-labeled L-cells. The 300-350-kDa 9S untransformed murine glucocorticoid receptor complex is composed of a 100-kDa steroid-binding phosphoprotein and one or possibly two units of the 90-kDa heat shock protein (hsp90), which is also a phosphoprotein. Transformation of this complex to the 4S DNA-binding state is accompanied by dissociation of hsp90. When receptors in cytosol are transformed by heating at 25°C, there is no gross change in the degree of phosphorylation of the steroid-binding protein. Both receptors that are bound to DNA after transformation under cell-free conditions and receptors that are located in the nucleus of cells incubated at 37°C in the presence of glucocorticoid are labeled with 32P. The results of experiments in which the 32P-labeled receptor was submitted to limited proteolysis suggest that the 16-kDa DNA-binding domain is phosphorylated and that the 28-kDa steroid-binding domain is not.

Original languageEnglish (US)
Pages (from-to)215-225
Number of pages11
JournalJournal of Steroid Biochemistry
Issue number1-3
StatePublished - 1987

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology


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