Fatty acid binding proteins shape the cellular response to activation of the glucocorticoid receptor
Liu, B.; Chandrashekaran, I. R.; Ilyichova, O.; Valour, D.; Melchiore, F.; Bourrier, C.; Giganti, A.; Stephan, J.-P.; Dacquet, C.; Genissel, P.; Gosgnach, W.; Weaver, R. J.; Porter, C. J.; Scanlon, M. J.; Halls, M. L.
Show abstract
Glucocorticoids are steroid hormones that are essential for life in mammals. Therapeutically, they are some of the most cost-effective drugs for the treatment of inflammatory diseases ranging from skin rashes to COVID-19, but their use is limited by adverse effects. Glucocorticoids exert their effects via the glucocorticoid receptor, a type I nuclear hormone receptor which modulates gene expression. The transcriptional activity of some related, but nuclear restricted, type II nuclear hormone receptors can be enhanced by a family of intracellular transport proteins, the fatty acid binding proteins (FABPs). We find that the transcriptional activity of the GR can be altered by a sub-set of FABP family members dependent on the GR-ligand. The ability of some FABPs to selectively promote or limit the transcriptional activity of the GR in a ligand-dependent manner could facilitate the discovery of drugs that narrow GR activity to only the desired subset of therapeutically relevant genes.
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