Publication | Open Access
Histone H2B monoubiquitination is a critical epigenetic switch for the regulation of autophagy
50
Citations
44
References
2016
Year
MitophagyDeubiquitinase Usp44Epigenetic ChangeGeneticsEpigenetic PathwaysEpigeneticsCell AutophagyCritical Epigenetic SwitchCell RegulationAutophagyCellular Regulatory MechanismLipophagyProtein DegradationHistone H2b MonoubiquitinationGene ExpressionEpigenetic RegulationCell BiologyChromatinChromatin RemodelingNatural SciencesEpigenomicsH2b MonoubiquitinationSystems BiologyMedicine
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.
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