Histone H2B monoubiquitination is a critical epigenetic switch for the regulation of autophagy

被引:45
作者
Chen, Su [1 ,2 ,3 ]
Jing, Yuanya [1 ]
Kang, Xuan [1 ]
Yang, Lu [4 ]
Wang, Da-Liang [5 ]
Zhang, Wei [1 ]
Zhang, Lei [1 ]
Chen, Ping [1 ]
Chang, Jian-Feng [1 ]
Yang, Xiao-Mei [1 ]
Sun, Fang-Lin [1 ]
机构
[1] Tongji Univ, Sch Life Sci & Technol, Res Ctr Translat Med, East Hosp,Adv Inst Translat Med, Shanghai 200092, Peoples R China
[2] Xi An Jiao Tong Univ, Sch Forens Sci, Hlth Sci Ctr, Xian 710061, Shaanxi, Peoples R China
[3] Peoples Hosp Zunhua, Dept Sci & Educ, Tangshan 064200, Hebei, Peoples R China
[4] Xi An Jiao Tong Univ, Res Ctr Translat Med, Affiliated Hosp 1, Xian 710061, Shaanxi, Peoples R China
[5] Tsinghua Univ, Sch Med, Beijing 100084, Peoples R China
基金
中国国家自然科学基金;
关键词
STEM-CELL DIFFERENTIATION; E3 UBIQUITIN LIGASE; NUCLEAR RECEPTORS; H3K4; METHYLATION; ROLES; ACTIVATION; UBIQUITYLATION; TRIMETHYLATION; TRANSCRIPTION; COACTIVATOR;
D O I
10.1093/nar/gkw1025
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Autophagy is an evolutionarily conserved cellular process that primarily participates in lysosomemediated protein degradation. Although autophagy is a cytoplasmic event, how epigenetic pathways are involved in the regulation of autophagy remains incompletely understood. Here, we found that H2B monoubiquitination (H2Bub1) is down-regulated in cells under starvation conditions and that the decrease in H2Bub1 results in the activation of autophagy. We also identified that the deubiquitinase USP44 is responsible for the starvation-induced decrease in H2Bub1. Furthermore, the changes in H2Bub1 affect the transcription of genes involved in the regulation of autophagy. Therefore, this study reveals a novel epigenetic pathway for the regulation of autophagy through H2Bub1.
引用
收藏
页码:1144 / 1158
页数:15
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