西亚试剂：GSK3-TIP60-ULK1 Signaling Pathway Links Growth Factor Depri

GSK3-TIP60-ULK1 Signaling Pathway Links Growth Factor Deprivation to Autophagy

Shu-Yong Lin1,*, Terytty Yang Li1,*, Qing Liu1, Cixiong Zhang1, Xiaotong Li1, Yan Chen1, Shi-Meng Zhang2, Guili Lian1, Qi Liu1, Ka Ruan1, Zhen Wang1, Chen-Song Zhang1, Kun-Yi Chien3, Jiawei Wu4, Qinxi Li1, Jiahuai Han1, Sheng-Cai Lin1,†

In metazoans, cells depend on extracellular growth factors for energy homeostasis. We found that glycogen synthase kinase-3 (GSK3), when deinhibited by default in cells deprived of growth factors, activates acetyltransferase TIP60 through phosphorylating TIP60-Ser86, which directly acetylates and stimulates the protein kinase ULK1, which is required for autophagy. Cells engineered to express TIP60S86A that cannot be phosphorylated by GSK3 could not undergo serum deprivation–induced autophagy. An acetylation-defective mutant of ULK1 failed to rescue autophagy in ULK1−/− mouse embryonic fibroblasts. Cells used signaling from GSK3 to TIP60 and ULK1 to regulate autophagy when deprived of serum but not glucose. These findings uncover an activating pathway that integrates protein phosphorylation and acetylation to connect growth factor deprivation to autophagy.

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