自噬
自噬相关蛋白13
细胞生物学
乙酰化
ULK1
蛋白激酶A
ATG8型
袋3
生物
乙酰转移酶
化学
生物化学
磷酸化
蛋白质磷酸化
细胞凋亡
安普克
基因
作者
Shu‐Yong Lin,Terytty Yang Li,Qing Liu,Cixiong Zhang,Xiaotong Li,Yan Chen,Shimeng Zhang,Guili Lian,Qi Liu,Ka Ruan,Zhen Wang,Chen‐Song Zhang,Kun‐Yi Chien,Jiawei Wu,Qinxi Li,Jiahuai Han,Shu‐Yong Lin
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2012-04-27
卷期号:336 (6080): 477-481
被引量:324
标识
DOI:10.1126/science.1217032
摘要
Acetylation and Autophagy Autophagy allows cells to digest their own components when necessary to survive stressful conditions. Lin et al. (p. 477) and Yi et al. (p. 474) describe signaling mechanisms in mammalian cells and yeast, respectively, by which autophagy is regulated by protein acetylation. In mammalian cells deprived of serum, the acetyltransferase TIP60 was activated by phosphorylation by the protein kinase GSK3 (glycogen synthase kinase 3). TIP60's target appeared to be a protein kinase central to autophagy regulation, ULK1. This activating pathway was required for autophagy in the absence of serum, but was not needed for autophagy in cells deprived of glucose. In the yeast Saccharomyces cerevisiae starved of nitrogen, another acetylation mechanism was uncovered. Starvation led to activation of the histone acetyltransferase Esa1, which acetylated the protein Atg3, a key component of the autophagy machinery, thus increasing its interaction with another autophagy protein, Atg8.
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