Abstract

This proposal focuses on the relationship between glucocorticoid receptor (GR) function and dynamic transformations of GR by phosphorylation and association with heat shock proteins. Previous work by the principal investigator has identified in detail the sites at which GR is phosphorylated, and has shown cell-cycle dependent changes in GR phosphorylation and heat shock protein association/dissociation. The present proposal will extend these studies, addressing 1) the role of GR phosphorylation in GR function; 2) the role of cell-cycle dependent kinases in this phosphorylation; 3) the possibility that estrogen in progesterone receptors also traverse ATP-dependent cycles.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
5R01DK003535-37
Application #
2430168
Study Section
Endocrinology Study Section (END)
Program Officer
Margolis, Ronald N
Project Start
1977-09-30
Project End
2000-05-31
Budget Start
1997-06-01
Budget End
1998-05-31
Support Year
37
Fiscal Year
1997
Total Cost
Indirect Cost

  Institution

Name
Dartmouth College
Department
Physiology
Type
Schools of Medicine
DUNS #
041027822
City
Hanover
State
NH
Country
United States
Zip Code
03755

  Publications

Sheldon, L A; Becker, M; Smith, C L (2001) Steroid hormone receptor-mediated histone deacetylation and transcription at the mouse mammary tumor virus promoter. J Biol Chem 276:32423-6
Sapolsky, R M; Romero, L M; Munck, A U (2000) How do glucocorticoids influence stress responses? Integrating permissive, suppressive, stimulatory, and preparative actions. Endocr Rev 21:55-89
Bodwell, J; Swiff, F; Richardson, J (1999) Long duration electroporation for achieving high level expression of glucocorticoid receptors in mammalian cell lines. J Steroid Biochem Mol Biol 68:77-82
Richardson, J; Vinson, C; Bodwell, J (1999) Cyclic adenosine-3',5'-monophosphate-mediated activation of a glutamine synthetase composite glucocorticoid response element. Mol Endocrinol 13:546-54
Sheldon, L A; Smith, C L; Bodwell, J E et al. (1999) A ligand binding domain mutation in the mouse glucocorticoid receptor functionally links chromatin remodeling and transcription initiation. Mol Cell Biol 19:8146-57
Bodwell, J E; Webster, J C; Jewell, C M et al. (1998) Glucocorticoid receptor phosphorylation: overview, function and cell cycle-dependence. J Steroid Biochem Mol Biol 65:91-9
Croteau, W; Bodwell, J E; Richardson, J M et al. (1998) Conserved cysteines in the type 1 deiodinase selenoprotein are not essential for catalytic activity. J Biol Chem 273:25230-6
Hu, J M; Bodwell, J E; Munck, A (1997) Control by basal phosphorylation of cell cycle-dependent, hormone-induced glucocorticoid receptor hyperphosphorylation. Mol Endocrinol 11:305-11
Webster, J C; Jewell, C M; Bodwell, J E et al. (1997) Mouse glucocorticoid receptor phosphorylation status influences multiple functions of the receptor protein. J Biol Chem 272:9287-93
Bodwell, J E; Hu, J M; Hu, L M et al. (1996) Glucocorticoid receptors: ATP and cell cycle dependence, phosphorylation, and hormone resistance. Am J Respir Crit Care Med 154:S2-6

Showing the most recent 10 out of 26 publications