Journal
EUROPEAN JOURNAL OF IMMUNOLOGY
Volume 43, Issue 12, Pages 3167-3174Publisher
WILEY
DOI: 10.1002/eji.201343752
Keywords
C-type lectin; Macrophage C-type Lectin (MCL); Mincle; Myeloid cells; Signaling adaptor
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Funding
- University of Oslo
- Norwegian Research Council, Norway
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Upon receptor activation, the myeloid C-type lectin receptor Mincle signals via the Syk-CARD9-Bcl10-MALT1 pathway. It does so by recruiting the ITAM-bearing Fc epsilon RI-. The related receptor macrophage C-type Lectin (MCL) has also been shown to be associated with Syk and to be dependent upon this signaling axis. We have previously shown that MCL co-precipitates with Fc epsilon RI-, but were unable to show a direct association, suggesting that MCL associates with Fc epsilon RI- via another molecule. Here, we have used rat primary cells and cell lines to investigate this missing link. A combination of flow cytometric and biochemical analysis showed that Mincle and MCL form heteromers on the cell surface. Furthermore, association with MCL and Fc epsilon RI- increased Mincle expression and enhanced phagocytosis of Ab-coated beads. The results presented in this paper suggest that the Mincle/MCL/Fc epsilon RI- complex is the functionally optimal form for these C-type lectin receptors on the surface of myeloid cells.
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