enzyme I interacts with RORs, but its effect is not yet known. Phosphorylation: Phosphorylation of RORα1, which inhibits its transcriptional activity, is induced by Protein Kinase C. ERK2: Extracellular signal-regulated kinase-2 also phosphorylates RORα. ATXN1: ATXN1 and RORα form part of a protein complex in Purkinje cells. FOXP3: FOXP3 directly represses the transcriptional activity of RORs. NME1: ROR has been shown to specifically interact with NME1. NM23-2: NM23-2 is a nucleoside diphosphate kinase involved in organogenesis and differentiation. NM23-1: NM23-1 is the product of a tumor metastasis suppressor candidate gene. As a drug target Because RORα and REV-ERBα are nuclear receptors that share the same target genes and are involved in processes that regulate metabolism, development, immunity, and circadian rhythm, they show potential as drug targets. Synthetic ligands have a variety of potential therapeutic uses, and can be used to treat diseases such as diabetes, atherosclerosis, autoimmunity, and cancer. T0901317 and SR1001, two synthetic ligands, have been found to be RORα and RORγ inverse agonists that suppress reporter activity and have been shown to delay onset and clinical severity of multiple sclerosis and other Th17 cell-mediated autoimmune diseases. SR1078 has been discovered as a RORα and RORγ agonist that increases the expression of G6PC and FGF21, yielding the therapeutic potential to treat obesity and diabetes as well as cancer of the breast, ovaries, and prostate. SR3335 has also been discovered as a RORα inverse agonist. CGP 52608 See also RAR-related orphan receptor REV-ERBα Aromatase deficiency References Further reading External links Intracellular receptors Transcription factors