Figure 2. Cbl-b mediates ubiquitination and degradation of Dectin-2 and Dectin-3. (A and B) Association analyses of Cbl-b with Dectin-2 or Dectin-3 in mouse BMDMs, which were stimulated with C. albicans hyphae for the indicated times. (C and D) Hyphae-induced ubiquitination of Dectin-2 and Dectin-3 in WT and Cbl-b–deficient BMDMs. (E) Hyphae-induced degradation of Dectin-2 and Dectin-3 in WT and Cbl-b–deficient BMDMs. (F) Hyphae-induced degradation of Mincle, Syk, and SHP-2 in WT and Cbl-b–deficient BMDMs. Cell lysates were immunoprecipitated with anti–Dectin-2 or –Dectin-3 antibodies as indicated. The cell lysate and immunoprecipitates were subjected to immunoblotting using the indicated antibodies. (G and H) Surface expression levels of Dectin-2 (G) or Dectin-3 (H) in WT and Cbl-b–deficient BMDMs, which were stimulated with C. albicans hyphae (MOI = 1) for the indicated times. BMDMs were incubated with anti–Dectin-2, anti–Dectin-3, or isotype control IgG for 30 min at 4°C and then stained with FITC-labeled goat anti–mouse secondary antibodies. Samples were then examined for FITC intensity by flow cytometry. The data shown are representative of three independent and reproducible experiments. IP, immunoprecipitation; Iso, isotype; Ly, lysis.
Figure 2.

Cbl-b mediates ubiquitination and degradation of Dectin-2 and Dectin-3. (A and B) Association analyses of Cbl-b with Dectin-2 or Dectin-3 in mouse BMDMs, which were stimulated with C. albicans hyphae for the indicated times. (C and D) Hyphae-induced ubiquitination of Dectin-2 and Dectin-3 in WT and Cbl-b–deficient BMDMs. (E) Hyphae-induced degradation of Dectin-2 and Dectin-3 in WT and Cbl-b–deficient BMDMs. (F) Hyphae-induced degradation of Mincle, Syk, and SHP-2 in WT and Cbl-b–deficient BMDMs. Cell lysates were immunoprecipitated with anti–Dectin-2 or –Dectin-3 antibodies as indicated. The cell lysate and immunoprecipitates were subjected to immunoblotting using the indicated antibodies. (G and H) Surface expression levels of Dectin-2 (G) or Dectin-3 (H) in WT and Cbl-b–deficient BMDMs, which were stimulated with C. albicans hyphae (MOI = 1) for the indicated times. BMDMs were incubated with anti–Dectin-2, anti–Dectin-3, or isotype control IgG for 30 min at 4°C and then stained with FITC-labeled goat anti–mouse secondary antibodies. Samples were then examined for FITC intensity by flow cytometry. The data shown are representative of three independent and reproducible experiments. IP, immunoprecipitation; Iso, isotype; Ly, lysis.

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