| First Author | Chen S | Year | 2017 |
| Journal | Nucleic Acids Res | Volume | 45 |
| Issue | 3 | Pages | 1144-1158 |
| PubMed ID | 28180298 | Mgi Jnum | J:250278 |
| Mgi Id | MGI:5922158 | Doi | 10.1093/nar/gkw1025 |
| Citation | Chen S, et al. (2017) Histone H2B monoubiquitination is a critical epigenetic switch for the regulation of autophagy. Nucleic Acids Res 45(3):1144-1158 |
| abstractText | Autophagy is an evolutionarily conserved cellular process that primarily participates in lysosome-mediated 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. |
