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Beschreibung

Glucocorticoid receptor (Uniprot P06536, also known as GR, Nuclear receptor subfamily 3 group C member 1) is encoded by Nr3c1 (also known as Grl, Grc) gene (Gene ID: 24413) in rat species. It has a dual mode of action whereby it acts as a transcription factor that binds to glucocorticoid response elements, both for nuclear and mitochondrial DNA, and also acts a modulator of other transcription factors. GR is composed of several conserved structural elements, including a carboxy-terminal ligand-binding domain (which contains residues critical for receptor dimerization and hormone-dependent gene transactivation), a neighboring hinge region containing nuclear localization signals, a central zinc-finger-containing DNA-binding domain, and an amino-terminal variable region that participates in ligand-independent gene transcription. In the absence of hormone, a significant population of GR is localized to the cytoplasm in an inactive form via its association with regulatory chaperone proteins, such as HSP90, HSP70, and FKBP52. Upon hormone binding, GR is released from the chaperone complex and translocates to the nucleus as a dimer to associate with glucocorticoid response elements (GREs), thereby enhancing or repressing transcription of specific target genes. GR-mediated transcriptional activation is modulated by phosphorylation and upon binding to receptor agonist it becomes hyperphosphorylated. Although basal GR phosphorylation at Ser155 and Ser287 is low, but it is highly inducible by BDNF treatment. It is been reported that BDNF-induced phosphorylation increases GR occupancy and cofactor recruitment at the promoter of a BDNF-enhanced gene.