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. 2017 Sep 25;6(9):e381. doi: 10.1038/oncsis.2017.80

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Copyright © 2017 The Author(s)

Oncogenesis is an open-access journal published by Nature Publishing Group. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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PRAS40 98-110 is sufficient but not required for PRAS40–P65 association. (a) The PRAS40 structure was predicted by the I-TASSER algorithm and visualized using the PyMOL software (Left). The truncations of PRAS40 were produced based on the predicted structure of PRAS40 (Right). ✓ means could interact with P65; × means could not interact with P65 according to the results of a GST co-precipitation assay (b, c). (b) Truncations of PRAS40 with GST tag protein were co-transfected withVenus-P65 (V-P65, P65 protein with the Venus-Flag tag). The GST, Venus and truncations of PRAS40 (1-23, 1-51,1-75 and 110-256) could not co-precipitate P65 (lanes 1–3). However, the full length of PRAS40 and the truncations, including 1-110, 1-125, 1-170, 75-256, 98-256, 23-256 and 44-256 of PRAS40, could co-precipitate P65. 14-3-3ζwas used as the positive control for PRAS40 binding in this experiment. (c) The small truncation 98-110 of PRAS40 could co-precipitate P65 (lane 2 vs lane 1). But it could not significantly affect the co-precipitation of P65 by full-length PRAS40 (lane 6 vs lane 5). Lanes 3 and 4 were negative controls. (d) The 98-100 truncation of PRAS40 did not significantly regulate NF-κB transcriptional activity with or without tumor necrosis factor-α (TNF-α) stimulation (20 ng/ml, 2 h). (e) The proteins in the 3κB-Luc group cells were blotted to validate the transfection.