Skip to main content
. 2020 Mar 13;295(16):5335–5349. doi: 10.1074/jbc.RA119.012260

Figure 1.

Figure 1.

PRR11 associates with and recruits Arp2/3 complex. a, mass spectrometry analysis of PRR11-associated proteins. Lysates from H1299 cells transfected with Flag-WT PRR11 or pcDNA3.0 (empty) were immunoprecipitated with anti-Flag and then analyzed by MS. Subunits of Arp2/3 complex (Arp2, Arp3, ARPC1A, ARPC1B, ARPC2, ARPC3, ARPC4, ARPC5, and ARPC5L) were identified in the PRR11 immunoprecipitates. b, and c, interaction between PRR11 and Arp2 was confirmed by coimmunoprecipitation. b, cells were transfected with plasmids encoding Flag-WT PRR11 or pcDNA3.0. Cell lysates were immunoprecipitated with Flag antibody and blotted with different antibodies as indicated. c, to verify the interaction of endogenous proteins, the lysate of cell was immunoprecipitated with Arp2 antibody. Co-immunoprecipitation (Co-IP) and whole-cell lysates (Input) were subjected to immunoblotting (IB) with different antibodies as indicated. d, endogenous PRR11 co-localizes with Arp2. Cells were fixed and stained for PRR11 and Arp2 antibody. Scale bars, 10 μm. White arrowhead indicates that Arp2 localizes at the lamellipodia, and zoomed images of the boxed region are shown at the bottom-left corner (scale bars, 1 μm). e, Western blot analysis for the indicated proteins in the pvN173- and WT PRR11-transfected cells. Cells were lysed 24 h after transfection and analyzed for the indicated proteins. GAPDH, glyceraldehyde-3-phosphate dehydrogenase.