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. 2021 Mar 2;53(3):369–383. doi: 10.1038/s12276-021-00570-6

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© The Author(s) 2021

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 Time-course analysis of ULK1 phosphorylation. The western blotting analysis was performed with S405 and S415 phospho-specific antibodies following insulin withdrawal. b Effect of GSK3B knockdown on ULK1 S405 and S415 phosphorylation after insulin withdrawal for 6 h. c In vitro kinase assay for ULK1 phosphorylation at S405 and S415. GST-tagged ULK1 fragments (amino acid residues 279–430) with mutations at S405A or S415A were used as substrates for HA-GSK3B-CA immunoprecipitation from HEK293 cells. The western blotting analysis was performed with S405 and S415 phospho-specific antibodies. d Effect of S405 or S415 phosphorylation on the phosphorylation of the other. The ULK1 WT, S405A, or S415A construct was expressed in sgUlk1 cells, and western blotting analysis using phospho-specific antibodies was performed after insulin withdrawal for 6 h. In all experiments, the blots shown are representative of at least three experiments with similar results.