Journal
BIOMOLECULES
Volume 9, Issue 3, Pages -Publisher
MDPI
DOI: 10.3390/biom9030095
Keywords
glucocorticoid receptor; phosphorylation; intrinsically disordered; transactivation activity; gene regulation; coactivators
Categories
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available