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. Author manuscript; available in PMC: 2014 May 1.
Published in final edited form as: Nature. 2013 Jul 17;500(7463):468–471. doi: 10.1038/nature12313

Figure 1. Autophagy is associated with reduced acetylation of histone H4 lysine 16.

Figure 1

(a) Starvation (3 h)-induced autophagy results in a downregulation of H4K16ac in histone extracts of MEF cells. (b) Upon rapamycin treatment (300 nM) LC3 conversion and downregulation of H4K16ac are observed in WT MEF cells but not in the autophagy-deficient Atg5−/− and Atg7−/− MEF cells. (c) Rapamycin treatment increased the LC3-II/LC3-I ratio and promoted H4K16ac decrease in Sirt1−/− and WT MEF cells. (d) Rapamycin-induced autophagy led to downregulation of H4K16ac at 48 h in histone extracts of HeLa and U20S cells, and after 6 h in U1810 cells. (e) Quantification of H4K16 acetylation by immunoblotting is depicted for rapamycin-treated cells. Data are expressed as mean ± SEM (n=3–5); *Pvalue<0.05; **Pvalue<0.01.