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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 2. — COMMD8 and COMMD3 are interdependent for stability. (A) IB analysis for the levels of COMMD8 and COMMD3 proteins in Fo B cells from Commd8Δ, Commd3Δ (Δ), and littermate control (Ctrl, Commd8^f/+Mb1^Cre/+ or Commd3^f/+Mb1^Cre/+) mice. The COMMD8 and COMMD3 levels in mutant cells are expressed as the ratio to their levels in control cells and normalized to GAPDH levels. (B) Quantitative PCR analysis for the levels of Commd8 (left) and Commd3 (right) mRNAs relative to Gapdh expression in Fo B cells from Commd8Δ, Commd3Δ (Δ), and littermate control (Ctrl, Commd8^f/+Mb1^Cre/+ or Commd3^f/+Mb1^Cre/+) mice. Data are shown as the mean + SD of triplicates and representative of three independent experiments. (C and D) IB analysis for the degradation of Myc-tagged COMMD8 (C) or COMMD3 (D) in vector-transfected control and COMMD3-deficient (sgCommd3; C) or COMMD8-deficient (sgCommd8; D) 2PK-3 cells at the indicated times after cycloheximide treatment. (E) IB analysis for the levels of Myc-tagged COMMD8 in sgCommd3 2PK-3 cells at the indicated times after treatment with MG132 or solvent DMSO in the presence of cycloheximide. (F and G) IB analysis for the K48-linked ubiquitination (Ub-K48) of Myc-tagged COMMD8 (F) or COMMD3 (G) in vector-transfected control (Ctrl) and sgCommd3 (sg3; F) or sgCommd8 (sg8; G) 2PK-3 cells. Data are representative of three independent experiments. Error bars represent the mean ± SD of three independent experiments, and representative blots are shown (A and C–E). *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001; ns, not significant. The P values were obtained by two-tailed paired (A) or unpaired (B–E) t test.