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. 2017 May 1;130(9):1596–1611. doi: 10.1242/jcs.195412

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© 2017. Published by The Company of Biologists Ltd

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.

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Fig. 3. — Analysis of BST2 interaction with NEDD4, MARCH8 and β-TrCP. (A) HEK293T cells were transfected with plasmid encoding FLAG–BST2 or p3xFLAG vector (used as negative control) along with expression vectors for HA–NEDD4, HA–MARCH8 or HA–β-TrCP, or HA–WWP1 used as negative control. Binding of HA-tagged E3 ubiquitin ligases and FLAG–BST2 was assessed by immunoprecipitating (IP) FLAG–BST2 followed by western blot analyses. Left panels represent the input (lysates) and right panels represent bound proteins (FLAG-IP). Data are representative of four independent experiments. (B,C) NEDD4 and MARCH8 interact with BST2 independently of each other. HeLa cells transfected with the indicated siRNA were transfected with both plasmids encoding FLAG–BST2 and HA-tagged E3 ligases, followed by FLAG–BST2 pull-down. Binding of HA-tagged E3 ubiquitin ligases and FLAG–BST2 was analyzed by western blotting. Left panels represent the input and right panels represent bound proteins. Data are representative of three independent experiments.