The avian progesterone receptor is being used as a model for studying the role of phosphorylation in receptor structure and function. This receptor has been shown to be phosphorylated at multiple sites on serine residues. The present studies are designed to clearly described the extent to which the progesterone receptor is phosphorylated before and after progesterone treatment. Through peptide mapping experiments, the actual sites of phosphorylation will be determined within the primary structure of the receptor. There is now evidence for additional phosphorylation of the receptor following progesterone treatment in vivo. This will be described in detail as a receptor processing step that may relate to nuclear binding or regulation of gene expression. A cell-free system will be developed for studying this receptor processing which will allow the identification and characterization of all participating factors. These studies should provide a clear biochemical framework for assessing the significance of individual phosphorylation events to receptor activity.

Agency
National Institute of Health (NIH)
Institute
Eunice Kennedy Shriver National Institute of Child Health & Human Development (NICHD)
Type
Research Project (R01)
Project #
5R01HD018287-06
Application #
3315328
Study Section
Biochemical Endocrinology Study Section (BCE)
Project Start
1983-09-01
Project End
1990-08-31
Budget Start
1988-09-01
Budget End
1989-08-31
Support Year
6
Fiscal Year
1988
Total Cost
Indirect Cost
Name
Mayo Clinic, Rochester
Department
Type
DUNS #
City
Rochester
State
MN
Country
United States
Zip Code
55905
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Schowalter, D B; Sullivan, W P; Maihle, N J et al. (1991) Characterization of progesterone receptor binding to the 90- and 70-kDa heat shock proteins. J Biol Chem 266:21165-73
Kost, S L; Smith, D F; Sullivan, W P et al. (1989) Binding of heat shock proteins to the avian progesterone receptor. Mol Cell Biol 9:3829-38
Sullivan, W P; Madden, B J; McCormick, D J et al. (1988) Hormone-dependent phosphorylation of the avian progesterone receptor. J Biol Chem 263:14717-23
Dougherty, J J; Rabideau, D A; Iannotti, A M et al. (1987) Identification of the 90 kDa substrate of rat liver type II casein kinase with the heat shock protein which binds steroid receptors. Biochim Biophys Acta 927:74-80
Puri, R K; Toft, D O (1986) Peptide mapping analysis of the avian progesterone receptor. J Biol Chem 261:5651-7