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. 2017 Apr 19;8(6):726–734. doi: 10.1111/jdi.12651

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© 2017 The Authors. Journal of Diabetes Investigation published by Asian Association for the Study of Diabetes (AASD) and John Wiley & Sons Australia, Ltd

This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

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Structure and regulation of forkhead box class O family member proteins (FoxOs). (a) Schematic diagram showing the different domains that characterize human FoxOs. FoxOs share a highly conserved forkhead deoxyribonucleic acid‐binding domain (FHD), which binds to conserved sequences in the target genes. Acetylation and phosphorylation sites are depicted only in FoxO1 as a representative. (b) A model for FoxO1 regulation through insulin‐induced and phosphorylation‐dependent degradation. A, acetylation site; aa, amino acids; NES, nuclear export sequence; NLS, nuclear localization sequence; P, phosphorylation site; TAD, transactivation domain.