Glycogen synthase kinase 3 drives thymocyte egress by suppressing β-catenin activation of Akt
Chenfeng Liu, Lei Ma, Yuxuan Wang, Jiayi Zhao, Pengda Chen, Xian Chen, Yingxin Wang, Yanyan Hu, Yun Liu, Xian Jia, Zhang‐Hua Yang, Xingzhi Yin, Jianfeng Wu, Suqin Wu, Haiping Zheng, Xiaohong Ma, Xiufeng Sun, Ying He, Lianghua Lin, Yubing Fu, Kunyu Liao, Xiaojuan Zhou, Shan Jiang, Guofeng Fu, Jian Tang, Wei Han, Xiao Lei Chen, Wenzhu Fan, Yazhen Hong, Jiahuai Han, Xiangyang Huang, Boan Li, Nengming Xiao, Changchun Xiao, Guo Fu, Wen‐Hsien Liu
Abstract
expression, thereby preventing emigration of thymocytes. A cytoplasmic membrane-localized β-catenin excluded from the nucleus promoted Akt activation, suggesting a new function of β-catenin independent of its role as a transcriptional activator. Furthermore, genetic ablation of β-catenin, retroviral expression of a dominant negative Akt mutant, and transgenic expression of a constitutively active Foxo1 restored emigration of GSK3-deficient thymocytes. Our findings establish an essential role for GSK3 in thymocyte egress and reveal a previously unidentified signaling function of β-catenin in the cytoplasm.