Literature DB >> 6712701

Phosphorylation in vivo of rat hepatic glucocorticoid receptor.

P Grandics, A Miller, T J Schmidt, G Litwack.   

Abstract

Rat liver glucocorticoid receptors were labeled in vivo with [32P]orthophosphate. In the last two fractionation procedures leading to purified, molybdate-stabilized, unactivated receptor complex, bound [32P] coeluted with peaks of bound [3H]triamcinolone acetonide. SDS-gel electrophoresis revealed [32P] labeled 90K and 24K bands. The lower molecular weight band is heavily phosphorylated and it could be either a component of the unactivated receptor or a degradation product.

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Year:  1984        PMID： 6712701     DOI： 10.1016/0006-291x(84)91413-x

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  4 in total

1.  Mitogen-activated and cyclin-dependent protein kinases selectively and differentially modulate transcriptional enhancement by the glucocorticoid receptor.

Authors:  M D Krstic; I Rogatsky; K R Yamamoto; M J Garabedian
Journal:  Mol Cell Biol       Date:  1997-07       Impact factor: 4.272

2.  Ligand and DNA-dependent phosphorylation of human progesterone receptor in vitro.

Authors:  M K Bagchi; S Y Tsai; M J Tsai; B W O'Malley
Journal:  Proc Natl Acad Sci U S A       Date:  1992-04-01       Impact factor: 11.205

3.  Phosphorylation of immunopurified rat liver glucocorticoid receptor by the catalytic subunit of cAMP-dependent protein kinase.

Authors:  T Haske; M Nakao; V K Moudgil
Journal:  Mol Cell Biochem       Date:  1994-03-30       Impact factor: 3.396

4.  Protein kinase activity associated with the purified rat hepatic glucocorticoid receptor.

Authors:  A Miller-Diener; T J Schmidt; G Litwack
Journal:  Proc Natl Acad Sci U S A       Date:  1985-06       Impact factor: 11.205
  4 in total

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