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Role of Phosphorylation in the Modulation of the Glucocorticoid Receptor’s Intrinsically Disordered Domain

1
Department of Medical Education, Geisinger Commonwealth School of Medicine, Scranton, PA 18509, USA
2
Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, USA
*
Authors to whom correspondence should be addressed.
Biomolecules 2019, 9(3), 95; https://doi.org/10.3390/biom9030095
Received: 22 December 2018 / Revised: 18 February 2019 / Accepted: 21 February 2019 / Published: 11 March 2019
(This article belongs to the Special Issue Intrinsically Disordered Proteins and Chronic Diseases)
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Abstract

Protein phosphorylation often switches cellular activity from one state to another, and this post-translational modification plays an important role in gene regulation by the nuclear hormone receptor superfamily, including the glucocorticoid receptor (GR). Cell signaling pathways that regulate phosphorylation of the GR are important determinants of GR actions, including lymphoid cell apoptosis, DNA binding, and interaction with coregulatory proteins. All major functionally important phosphorylation sites in the human GR are located in its N-terminal domain (NTD), which possesses a powerful transactivation domain, AF1. The GR NTD exists as an intrinsically disordered protein (IDP) and undergoes disorder-order transition for AF1’s efficient interaction with several coregulatory proteins and subsequent AF1-mediated GR activity. It has been reported that GR’s NTD/AF1 undergoes such disorder-order transition following site-specific phosphorylation. This review provides currently available information regarding the role of GR phosphorylation in its action and highlights the possible underlying mechanisms of action. View Full-Text
Keywords: glucocorticoid receptor; phosphorylation; intrinsically disordered; transactivation activity; gene regulation; coactivators glucocorticoid receptor; phosphorylation; intrinsically disordered; transactivation activity; gene regulation; coactivators
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Kumar, R.; Thompson, E.B. Role of Phosphorylation in the Modulation of the Glucocorticoid Receptor’s Intrinsically Disordered Domain. Biomolecules 2019, 9, 95.

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