BRD7 increases phosphorylation of glycogen synthase kinase 3β (GSK3β) in response to activation of the insulin receptor-signaling pathway shortly after insulin stimulation and the nutrient-sensing pathway after feeding. BRD7 mediates phosphorylation of GSK3β at the Serine 9 residue and this effect on GSK3β occurs even in the absence of AKT activity.
BRD7 mediates phosphorylation of ribosomal protein S6 kinase (S6K) and leads to increased phosphorylation of the eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1) and, therefore, relieves its inhibition of the eukaryotic translation initiation factor 4E (eIF4E). The increase in phosphorylation of 4E-BP1 with BRD7 overexpression is blunted in the absence of AKT activity.
BRD7 interacts with the regulator subunits of PI3K, p85s, and increases the nuclear translocation of p85s.
BRD7 expression levels are reduced in the liver of obese mice and reinstating BRD7 leves in the liver improves glucose homeostasis in obese and diabetic mouse models.