PMID: 18407126Jan 1, 1993Paper

Progesterone receptor phosphorylation complexities in defining a functional role

Trends in Endocrinology and Metabolism : TEM
G S Takimoto, Kathryn B Horwitz

Abstract

All steroid receptors are phosphoproteins and several, including progesterone receptors (PRs), become hyperphosphorylated upon binding of ligand. PR phosphorylation is complex, occurring in different cellular compartments and perhaps requiring multiple serine kinases. A model that is emerging proposes that PR phosphorylation is progressive, occurring in at least a three-stage cascade. However, the functional significance of this phosphorylation cascade remains unclear.

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Citations

May 1, 1995·Trends in Endocrinology and Metabolism : TEM·D P McDonnell
Aug 29, 2003·The Journal of Steroid Biochemistry and Molecular Biology·Ming Qiu, Carol A Lange
Feb 3, 2000·Proceedings of the National Academy of Sciences of the United States of America·C A LangeK B Horwitz
Oct 22, 2008·Reproduction : the Official Journal of the Society for the Study of Fertility·Ana GordonJosé E Sánchez-Criado
Oct 30, 2007·The Journal of Steroid Biochemistry and Molecular Biology·Carol A Lange
May 1, 2015·Reproduction : the Official Journal of the Society for the Study of Fertility·Ana GordonJosé E Sánchez-Criado
Apr 1, 1994·Molecular and Cellular Endocrinology·G G Kuiper, A O Brinkmann
Jun 7, 1996·The Journal of Biological Chemistry·G S TakimotoK B Horwitz

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