Phosphorylation of purified glucocorticoid receptor from rat liver by an endogenous protein kinase

Kurl, Rabinder N.; Jacob, Samson T.

doi:10.1016/s0006-291x(84)80307-1

Cited by 65 publications

(17 citation statements)

References 15 publications

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“…However, it was not until much later that the first direct demonstration of GR phosphorylation was published in intact mouse L-cells cultured with [ 32 P]orthophosphate (9). In addition, GR isolated from rat liver cytosol was shown to be phosphorylated in vitro (10). These studies represent early evidence that GR was phosphorylated on one or more serine residues and gave way to further research on the phosphostatus of the GR.…”

Section: A Brief History Of Gr Phosphorylationmentioning

confidence: 56%

Emerging roles of glucocorticoid receptor phosphorylation in modulating glucocorticoid hormone action in health and disease

2009

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SummaryGlucocorticoids (GCs) are hormones naturally released when the body perceives stress and function to return homeostatic balance within various tissues. Synthetic GCs are widely prescribed therapeutics for the treatment of numerous inflammatory disorders and cancers. The effects of GCs are mediated by their binding and activation of the GC receptor (GR), a transcription factor that is subject to hormone-dependent and -independent phosphorylation on several serine and threonine residues. The GR is phosphorylated by kinases such as MAPKs, CDKs, and GSK-3b, and these modifications modulate the transcriptional activity of the GR within cells. Here, we discuss the phosphorylation status of the GR as a mechanism to dictate how cells will ultimately respond to GCs. In doing so, we will review current knowledge about each phosphorylated residue within the GR and their contributions to modulating GC signaling in normal homeostatic physiology and during the progression of disease.2009 IUBMB IUBMB Life, 61(10): 979-986, 2009

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Section: A Brief History Of Gr Phosphorylationmentioning

confidence: 56%

Emerging roles of glucocorticoid receptor phosphorylation in modulating glucocorticoid hormone action in health and disease

2009

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“…There is evidence that that differential phosphorylation is a potential regulator of species-specific actions of the GR (6,25,31,32). It has been shown that p38 MAPK is a component of the glucocorticoid-evoked pathway to lymphoid cell apoptosis in human and mouse cell systems and that the p38-specific upstream kinase kinase MKK3 appears to be involved.…”

Section: Discussionmentioning

confidence: 99%

Site-Specific Phosphorylation Induces Functionally Active Conformation in the Intrinsically Disordered N-Terminal Activation Function (AF1) Domain of the Glucocorticoid Receptor

Garza

Khan

Kumar

2010

Molecular and Cellular Biology

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Intrinsically disordered (ID) regions are disproportionately higher in cell signaling proteins and are predicted to have much larger frequency of phosphorylation sites than ordered regions, suggesting an important role in their regulatory capacity. In this study, we show that AF1, an ID activation domain of the glucocorticoid receptor (GR), adopts a functionally folded conformation due to its site-specific phosphorylation by p38 mitogen-activated protein kinase, which is involved in apoptotic and gene-inductive events initiated by the GR. Further, we show that site-specific phosphorylation-induced secondary and tertiary structure formation specifically facilitates AF1's interaction with critical coregulatory proteins and subsequently its transcriptional activity. These data demonstrate a mechanism through which ID activation domain of the steroid receptors and other similar transcription factors may adopt a functionally active conformation under physiological conditions.

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“…Evidence of steroid receptor phosphorylation has been demonstrated for the glucocorticoid (23), androgen (24), and progesterone (25) receptors. Additionally, Aurrichio et al (9) have reported the phosphorylation of the ER from calf uteri and have localized the involved phosphatase in the cytosol and the responsible kinase in the nuclei.…”

mentioning

confidence: 99%

Nuclear estrogen receptor molecular heterogeneity in the mouse uterus.

Golding

Korach

1988

Proc. Natl. Acad. Sci. U.S.A.

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Phosphorylation of purified glucocorticoid receptor from rat liver by an endogenous protein kinase

Cited by 65 publications

References 15 publications

Emerging roles of glucocorticoid receptor phosphorylation in modulating glucocorticoid hormone action in health and disease

Emerging roles of glucocorticoid receptor phosphorylation in modulating glucocorticoid hormone action in health and disease

Site-Specific Phosphorylation Induces Functionally Active Conformation in the Intrinsically Disordered N-Terminal Activation Function (AF1) Domain of the Glucocorticoid Receptor

Nuclear estrogen receptor molecular heterogeneity in the mouse uterus.

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