Fig. 7: An intact DCAF-1 interaction domain is required for Vpr and DCAF1 to degrade PU.1.
From: HIV-1 Vpr combats the PU.1-driven antiviral response in primary human macrophages

A Immunoblot analysis of lysates from MDMs treated for five hours with the indicated virions. B Summary graph of PU.1 protein normalized to vinculin from MDMs incubated for five hours with the indicated viruses from A. Each point and matched color is representative of an independent donor. Statistical significance was determined using a mixed-effects analysis with Tukey’s multiple comparisons test. *p < 0.05. C Immunoblot analysis of lysates from HEK 293T cells transfected with the indicated expression construct and treatment as indicated with 10 µM MG132 or vehicle (Veh) control (DMSO). A GFP-expressing plasmid was included where indicated as control for transfection efficiency, n = 2. D Immunoblot analysis of lysates from MDMs preincubated for two hours with vehicle (Veh) or MG132 as indicated and then treated for five hours with the indicated virus as in part A. E Summary graph of PU.1 protein normalized to vinculin from MDMs treated for five hours with the indicated viruses from D. Statistical significance was determined using a mixed-effects analysis with Šidák’s multiple comparisons test. **p = 0.0073. Each point and matched color is representative of an independent donor. F Working model of PU.1 and TET2 interacting with Vpr and DCAF1 in macrophages. Source data are provided as a Source Data file.