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. 2016 Nov 10;18(1):16–25. doi: 10.1080/15384047.2016.1252880

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© 2017 The Author(s). Published with license by Taylor & Francis Group, LLC

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 2. — TRIM21 interacts with Par-4 via its PRY-SPRY domain. HCT-116 cells were co-transfected with Par-4 plasmid and different TRIM21 constructs for 48 hrs. Par-4 was immunoprecipitated from whole cell lysates using anti-Par-4 antibody and protein G magnetic beads. The proteins were eluted from the beads and a western blot analysis is performed using anti-TRIM21 antibody. (a) A diagram representing the various TRIM21 constructs that were used (b) Western blots demonstrating that when co-transfecting with the TRIM21 construct that does not contain the PRY-SPRY domain, TRIM21 does not interact with Par-4; in contrast, when co-transfecting with the TRIM21 constructs that contain the PRY-SPRY domain, TRIM21 does interact with Par-4.