Phosphorylation of purified glucocorticoid receptor from rat liver by an endogenous protein kinase

Glucocorticoid receptor was purified from rat liver cytosol using a dexamethasone affinity column. The receptor thus purified displayed a single protein band when subjected to SDS-polyacrylamide gel electrophoresis. It had a molecular weight of 90,000 which was consistent with the reported value for other glucocorticoid receptor preparations. Incubation of the purified preparation with [gamma 32P] ATP and Mg2+ resulted in transfer of [32P] to the receptor protein indicating the presence of an endogeneous protein kinase activity capable of phosphorylating the receptor molecule. Phosphorylation of the glucocorticoid receptor by the endogenous protein kinase might serve as a direct mechanism for the activation of the receptor.