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. 2017 Apr 24;6(4):e323. doi: 10.1038/oncsis.2017.18

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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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The PDK1-binding domain of TCRP1 is R93-S107 and T109-A124.(a) Motif analysis of TCRP1 was processed in Scansite database (http://scansite.mit.edu/), and showed that the 93–107 amino-acid and 109–124 amino-acid sequences in the TCRP1 were PDK1-binding motif (upper panel). Two vectors including the two TCRP1 mutant fragments were constructed named pEGFP-TCRP1/mut1 and pEGFP-TCRP1/mut2, respectively (lower panel). (b) NIH/3T3 cells were co-transfected with EGFP-TCRP1/mut1 and pDsred-PDK1, or EGFP-TCRP1/mut2 and pDsred-PDK1, the direct interaction between TCRP1/muts and PDK1 was determined by forster resonance energy transfer (FRET) assay. (c) NIH/3T3 cells were transfected with pEGFP-TCRP1/mut1, or pEGFP-TCRP1/mut2, total protein extracts were subjected to IP using TCRP1 antibody or control IgG, followed by WB with PDK1 antibody. Reciprocal IP was done using PDK1 antibody or control IgG, followed by WB with the TCRP1 antibody.