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. 2019 May 14;216(7):1630–1647. doi: 10.1084/jem.20181494

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© 2019 Nakai et al.

This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).

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Figure 1. — COMMD8 forms a complex with COMMD3 and interacts with chemoattractant receptors. (A) IP assay for the interaction between COMMD8 and COMMD3 in mouse spleen cells. (B) IB analysis for the membrane translocation of COMMD8 and COMMD3 in mouse spleen cells stimulated with CXCL12. (C) Confocal microscopy for the subcellular localization and colocalization of Flag-tagged CXCR4 (red) and Myc-tagged COMMD8 (green) in HEK293 cells before and at 1 min after CXCL12 treatment. Colocalization of the signals (arrowheads) was quantified by measurement of overlapping pixel numbers in each cell. Each symbol represents an individual cell, and bars indicate means (0 min, n = 20; 1 min, n = 20). Representative images are shown. Bar, 10 µm. (D) IP assay for the interaction of Myc-tagged COMMD8 with Flag-tagged CXCR4, CXCR5, CCR7, and EBI2 in 2PK-3 cells stimulated with their respective ligands: CXCL12, CXCL13, CCL19, and 7α,25-HC. (E) IP assay for the interaction of COMMD8 with CXCR4 in mouse primary B cells stimulated with CXCL12. Data are representative of three independent experiments (A) or pooled from three independent experiments (C). Error bars represent the mean ± SD of three (B and D) or four (E) independent experiments, and representative blots are shown. *, P < 0.05; **, P < 0.01; ***, P < 0.001. The P values were obtained by two-tailed paired t test in comparison with the protein levels at 0 min (B, D, and E) or two-tailed unpaired t test (C). coIP, coimmunoprecipitation; DIC, differential interference contrast.