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Mincle, the receptor for mycobacterial cord factor, forms a functional receptor complex with MCL and FcεRI-γ.

Authors: Lobato-Pascual, Ana  Saether, Per Christian  Fossum, Sigbjørn  Dissen, Erik  Daws, Michael R 
Citation: Lobato-Pascual A, etal., Eur J Immunol. 2013 Dec;43(12):3167-74. doi: 10.1002/eji.201343752. Epub 2013 Aug 26.
Pubmed: (View Article at PubMed) PMID:23921530
DOI: Full-text: DOI:10.1002/eji.201343752

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 FcεRI-γ. 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 FcεRI-γ, but were unable to show a direct association, suggesting that MCL associates with FcεRI-γ 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 FcεRI-γ increased Mincle expression and enhanced phagocytosis of Ab-coated beads. The results presented in this paper suggest that the Mincle/MCL/FcεRI-γ complex is the functionally optimal form for these C-type lectin receptors on the surface of myeloid cells.

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CRRD Object Information
CRRD ID: 13838792
Created: 2019-01-16
Species: All species
Last Modified: 2019-01-16
Status: ACTIVE



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