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. 2018 Aug 28;9(9):860. doi: 10.1038/s41419-018-0921-2

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — a Cells were serum-starved overnight and treated with TNFα for 30 min. Protein acetylation was determined by immunoprecipitation with anti-Hsp70 antibody followed by western blotting for an antibody recognizing internal acetyl-lysine residues or anti-Hsp70 antibody. β-Actin was used as a protein loading control. b Cells were treated as described in (a) and lysates were detected by immunoprecipitation as described in the figure. c Cells were transiently cotransfected with HA-ARD1 or Flag Ctrl, Flag vector, Flag-Hsp70 WT, Flag-Hsp70 mutants, serum-starved overnight, and then treated with TNFα for 1 h. Cell lysates were lysed for the detection of the expression of the protein shown in the figure. The association between Vsp34 and Beclin-1 was analyzed by immunoprecipitation with anti-Beclin-1 antibody followed by western blotting for anti-Vsp34 or anti-Hsp70 antibodies