NEUROSCIENCE. Correction for “Sulfhydration of AKT triggers Tau-phosphorylation by activating glycogen synthase kinase 3β in Alzheimer’s disease,” by Tanusree Sen, Pampa Saha, Tong Jiang, and Nilkantha Sen, which was first published February 12, 2020; 10.1073/pnas.1916895117 (Proc. Natl. Acad. Sci. U.S.A. 117, 4418–4427).
The authors note that Fig. 2 appeared incorrectly. The corrected figure and its legend appear below. The online version has been corrected.
Fig. 2.
Phosphorylation of GSK3β is dependent on H2S. (A) Western blot analysis using brain tissue lysates of AD patients showed that AKT phosphorylation at S473 (AKT-S473P) and T308 (AKT-T308P) remains unaltered, but phosphorylation of GSK3β at S9 (GSK3β S9P) was decreased significantly. (B) Phosphorylation of AKT at S473 (AKT-S473P) and T308 (AKT-T308P) remains unaltered but phosphorylation of GSK3β at S9 (GSK3β S9P) was decreased in the cortex and hippocampus of PS19 mice analyzed by Western blot. (C) Administration of IL-1β in CBS+/− mice overexpressing hTau-P301L rescued phosphorylation of GSK3β at S9 (GSK3β S9P) compared to CBS+/+ mice overexpressing hTau-P301L. (D) Western blot analysis showed that depletion of CBS after administration of CBS RNAi in PS19 mice rescued phosphorylation of GSK3β at S9 (GSK3β S9P) although AKT phosphorylation at S473 (AKT-S473P) and T308 (AKT-T308P) remained unaltered. (E) The interaction between AKT and GSK3β was decreased in PS19 mice and analyzed by coimmunopreciptation (co-IP) analysis. (F) Administration of IL1β (10 ng) causes a decrease in the interaction between AKT and GSK3β in primary neuron culture. (G and H) Administration of GYY4137 (300 μM) causes a decrease in the interaction between AKT and GSK3β and the phosphorylation of GSK3β at S9 residue. (I) CBS+/+ or CBS−/− neurons overexpressing HA-AKT, HA-AKT-T308A/S473A, or HA-AKT-T308D/S473D were treated with IL-1β. Administration of IL-1β affects interaction between Akt and GSK3β and phosphorylation of GSK3β in CBS+/+ neurons compared to CBS−/− neurons.