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. 2021 Jan 5;11:1. doi: 10.1038/s41398-020-01158-w

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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 PIDD1 mutations do not disrupt autoprocessing. HEK293T cells were transiently transfected with the indicated FLAG-tagged variants of PIDD1 and analyzed by western blotting using either anti-FLAG-M2 or an anti-PIDD1-specific antibody. B Cell-based protein stability of mutant versus wild-type PIDD1. HEK293T cells were transiently transfected with vectors encoding FLAG-tagged PIDD1 wild-type (WT), and DD mutants Q863*, R815W, G876S, or the splice acceptor (SA) mutant. After 24 h the cells were treated with cycloheximide (CHX), alone or in combination with the proteasomal inhibitor MG-132, for the times indicated, and were then processed for western blotting using and anti-FLAG antibody, in a 4-h chase experiment. A longer, 12 h chase experiment was also performed, and results shown in Fig. S1. Reprobing with an antibody-recognizing GAPDH, or CHK1, was done to confirm comparable protein loading. PIDD1-FL (*), -C (§), and –CC (#) are indicated.