All members of the steroid hormone receptor family are phosphoproteins. Additional phosphorylation occurs in the presence of hormone. This hormone-induced phosphorylation, which is 2- to 7-fold more than the basal phosphorylation, is a rapid process. All steroid receptors are phosphorylated at more than one single site. Most phosphorylation sites are located in the N-terminal domain, and phosphorylation occurs mainly on serine residues. Phosphorylation on threonine residues occurs in only a few cases. Phosphorylation on tyrosine residues has been found only for the estrogen receptor. Six different protein kinases are possibly involved in steroid receptor phosphorylation (estrogen receptor kinase; protein kinase A; protein kinase C; casein kinase II; DNA-dependent kinase; Ser-Pro kinases). Steroid receptor phosphorylation has been directly implicated in: activation of hormone binding, nuclear import of steroid receptors, modulation of binding to hormone response elements, and consequently in transcription activation.

Additional Metadata
Keywords Hormone receptor, Protein kinase, Protein phosphorylation, Steroid hormone, Transcription regulation
Persistent URL dx.doi.org/10.1016/0303-7207(94)90287-9, hdl.handle.net/1765/71449
Journal Molecular and Cellular Endocrinology
Citation
Kuiper, G.G.J.M, & Brinkmann, A.O. (1994). Steroid hormone receptor phosphorylation: Is there a physiological role?. Molecular and Cellular Endocrinology, 100(1-2), 103–107. doi:10.1016/0303-7207(94)90287-9