Steroid hormone receptor phosphorylation: Is there a physiological role?
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.
|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|
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