Journal
NUCLEIC ACIDS RESEARCH
Volume 45, Issue 3, Pages 1144-1158Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkw1025
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Funding
- 973 program of the Ministry of Science and Technology of China [2015CB856204, 2015CB964802, 2016YFA0100400, 2014CB964603, 2014CB965001]
- National Natural Science Foundation of China [91419304, 31330043, 31271534]
- Ministry of Science and Technology of China [2015CB856204, 2015CB964802, 2016YFA0100400, 2014CB964603, 2014CB965001]
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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.
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