Glucocorticoid receptor

Definition:

Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling. Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity).; [Isoform Alpha]: Has transcriptional activation and repression activity. Mediates glucocorticoid-induced apoptosis. Promotes accurate chromosome segregation during mitosis. May act as a tumor suppressor. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression (By similarity).; [Isoform Beta]: Acts as a dominant negative inhibitor of isoform Alpha. Has intrinsic transcriptional activity independent of isoform Alpha when both isoforms are coexpressed. Loses this transcription modulator function on its own. Has no hormone-binding activity. May play a role in controlling glucose metabolism by maintaining insulin sensitivity (By similarity). Reduces hepatic gluconeogenesis through down-regulation of PEPCK in an isoform Alpha-dependent manner. Directly regulates STAT1 expression in isoform Alpha-independent manner.; [Isoform Alpha-2]: Has lower transcriptional activation activity than isoform Alpha. Exerts a dominant negative effect on isoform Alpha trans-repression mechanism.; [Isoform GR-P]: Increases activity of isoform Alpha.; [Isoform Alpha-B]: More effective than isoform Alpha in transcriptional activation, but not repression activity.; [Isoform 10]: Has transcriptional activation activity.; [Isoform Alpha-C1]: Has transcriptional activation activity.; [Isoform Alpha-C2]: Has transcriptional activation activity.; [Isoform Alpha-C3]: Has highest transcriptional activation activity of all isoforms created by alternative initiation. Has transcriptional repression activity. Mediates glucocorticoid-induced apoptosis.; [Isoform Alpha-D1]: Has transcriptional activation activity.; [Isoform Alpha-D2]: Has transcriptional activation activity.; [Isoform Alpha-D3]: Has lowest transcriptional activation activity of all isoforms created by alternative initiation. Has transcriptional repression activity.

References:

[1]. Evangelia Charmandari, et al. A novel point mutation in the ligand-binding domain (LBD) of the human glucocorticoid receptor (hGR) causing generalized glucocorticoid resistance: the importance of the C terminus of hGR LBD in conferring transactivational activity. J Clin Endocrinol Metab. 2005 Jun;90(6):3696-705. [Content Brief]

[2]. C J Fryer, et al. Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. Nature. 1998 May 7;393(6680):88-91. [Content Brief]

[3]. Bo He, et al. Human Glucocorticoid Receptor β Regulates Gluconeogenesis and Inflammation in Mouse Liver. Mol Cell Biol. 2015 Dec 28;36(5):714-30. [Content Brief]

[4]. Géraldine Vitellius, et al. Three Novel Heterozygous Point Mutations of NR3C1 Causing Glucocorticoid Resistance. Hum Mutat. 2016 Aug;37(8):794-803. [Content Brief]

[5]. M R Yudt, et al. Molecular identification and characterization of a and b forms of the glucocorticoid receptor. Mol Endocrinol. 2001 Jul;15(7):1093-103. [Content Brief]

[6]. Ingrid K Bender, et al. Determinants of the heightened activity of glucocorticoid receptor translational isoforms. Mol Endocrinol. 2013 Sep;27(9):1577-87. [Content Brief]

[7]. C M Bamberger, et al. Glucocorticoid receptor beta, a potential endogenous inhibitor of glucocorticoid action in humans. J Clin Invest. 1995 Jun;95(6):2435-41. [Content Brief]

[8]. I Wu, et al. Selective glucocorticoid receptor translational isoforms reveal glucocorticoid-induced apoptotic transcriptomes. Cell Death Dis. 2013 Jan 10;4(1):e453. [Content Brief]

[9]. R H Oakley, et al. The human glucocorticoid receptor beta isoform. Expression, biochemical properties, and putative function. J Biol Chem. 1996 Apr 19;271(16):9550-9. [Content Brief]

[10]. Tomoshige Kino, et al. Glucocorticoid receptor (GR) beta has intrinsic, GRalpha-independent transcriptional activity. Biochem Biophys Res Commun. 2009 Apr 17;381(4):671-5. [Content Brief]

[11]. Laura C Matthews, et al. Glucocorticoid receptor regulates accurate chromosome segregation and is associated with malignancy. Proc Natl Acad Sci U S A. 2015 Apr 28;112(17):5479-84. [Content Brief]

[12]. Nick Z Lu, et al. Translational regulatory mechanisms generate N-terminal glucocorticoid receptor isoforms with unique transcriptional target genes. Mol Cell. 2005 Apr 29;18(3):331-42. [Content Brief]

[13]. Hana Cho, et al. Glucocorticoid receptor interacts with PNRC2 in a ligand-dependent manner to recruit UPF1 for rapid mRNA degradation. Proc Natl Acad Sci U S A. 2015 Mar 31;112(13):E1540-9. [Content Brief]

[14]. Yoshinori Taniguchi, et al. Glucocorticoid receptor-beta and receptor-gamma exert dominant negative effect on gene repression but not on gene induction. Endocrinology. 2010 Jul;151(7):3204-13. [Content Brief]

[15]. Anna-Maria G Psarra, et al. Glucocorticoids induce mitochondrial gene transcription in HepG2 cells: role of the mitochondrial glucocorticoid receptor. Biochim Biophys Acta. 2011 Oct;1813(10):1814-21. [Content Brief]

[16]. P de Lange, et al. Expression in hematological malignancies of a glucocorticoid receptor splice variant that augments glucocorticoid receptor-mediated effects in transfected cells. Cancer Res. 2001 May 15;61(10):3937-41. [Content Brief]

[17]. Evangelia Charmandari, et al. A novel point mutation in helix 11 of the ligand-binding domain of the human glucocorticoid receptor gene causing generalized glucocorticoid resistance. J Clin Endocrinol Metab. 2007 Oct;92(10):3986-90. [Content Brief]

[18]. Nancy Nader, et al. Circadian rhythm transcription factor CLOCK regulates the transcriptional activity of the glucocorticoid receptor by acetylating its hinge region lysine cluster: potential physiological implications. FASEB J. 2009 May;23(5):1572-83. [Content Brief]

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