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. 2020 May 18;27(11):3021–3036. doi: 10.1038/s41418-020-0558-4

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© The Author(s), under exclusive licence to ADMC Associazione Differenziamento e Morte Cellulare 2020

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. 5 — a Overexpression of LOXL1 in U87 cells reduced BAG2 ubiquitylation. An antibody against BAG2 was applied to enrich the BAG2 protein levels, and BAG2 ubiquitylation was then tested. b Depletion of LOXL1 in LN18 cells enhances BAG2 ubiquitylation. c Mutation of K186 to R186 decreased BAG2 ubiquitylation. U87 cells were transiently transfected with the corresponding plasmids. BAG2 was tagged with FLAG and then immunoprecipitated with an antibody against FLAG. d K186 in BAG2 was mutated to R186 in LN18 cells, and BAG2 ubiquitylation was then tested. e MS analysis identified BAG2 K186 ubiquitylation. The spectrum of the ubiquitylation-modified K186 peptide was identified with an m/z value of 623.33 and a SEQUEST XCorr value of 2.62. f, g Both LOXL1 enzymatic activity and D515 were required for preventing the ubiquitylation of BAG2 at K186 and stabilizing the BAG2 protein. h, i Prevention of BAG2 K186 ubiquitylation enhanced the antiapoptotic activity of glioma cells.