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. 2019 Sep 11;9:13097. doi: 10.1038/s41598-019-49229-3

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© The Author(s) 2019

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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SMG7 14-3-3-like domain mediates its interaction with Ser15-phosphorylated p53. (a) Schematic illustrating various SMG7 fragments and point mutants used in (b,c). FH represents a Flag and HA tag at the 5′ end of all constructs. (b) p53 binding to SMG7 in vitro. GST or GST-p53 fusion proteins were used in pulldown assays with purified FH-SMG7 (full length or fragments). (c) Cell extracts and α-Flag (SMG7) immunoprecipitates from U2OS cells stably expressing FH-SMG7 or mutants treated with etoposide (20 µM, 6 hours) were analyzed by western blot using antibodies as indicated. Red arrows denote various SMG7 fragment expression sizes which were identified using SMG7 and HA antibodies. (d) H1299 cells co-transfected with p53 and F-SMG7 or F-SMG7-K66E constructs were analyzed as in (c). (e) Cell extracts and α-p53 immunoprecipitates from control and irradiated cells were analyzed by western blot using antibodies as indicated (long and short exposures shown).