Fig. 7: Suggested model for the effect of K89 and K403 acetylation on activity and cellular functions of G6PD.
From: Acetylation-dependent coupling between G6PD activity and apoptotic signaling
Left: Acetylation of K89 enhances the catalytic activity of G6PD and promotes its ubiquitylation on residues K95/K97. Sirt1 and Sirt2 can potentially deacetylate AcK89. Right: K403 is acetylated by KAT9 (Wang et al.34) and CBP (this work) and deacetylated by Sirt2 (Wang et al.34 and this work) and Sirt1 (this work). Acetylation of K403 inhibits G6PD activity and promotes the interaction with p53, leading to the stabilization of p53 and induction of pro-apoptotic signaling. K403 acetylation also promotes Fyn-dependent phosphorylation of Y503, which can be partially inhibited by the interaction between K403-acetylated G6PD and p53. Y503 phosphorylation has no effect on K403 deacetylation by Sirt1 and Sirt2. Created with BioRender.com.
