PubMed:23921530 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/23921530","sourcedb":"PubMed","sourceid":"23921530","source_url":"https://www.ncbi.nlm.nih.gov/pubmed/23921530","text":"Mincle, the receptor for mycobacterial cord factor, forms a functional receptor complex with MCL and FcεRI-γ.\nUpon 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.","tracks":[{"project":"Allie","denotations":[{"id":"SS1_23921530_3_0","span":{"begin":297,"end":321},"obj":"expanded"},{"id":"SS2_23921530_3_0","span":{"begin":323,"end":326},"obj":"abbr"}],"relations":[{"id":"AE1_23921530_3_0","pred":"abbreviatedTo","subj":"SS1_23921530_3_0","obj":"SS2_23921530_3_0"}],"attributes":[{"subj":"SS1_23921530_3_0","pred":"source","obj":"Allie"},{"subj":"SS2_23921530_3_0","pred":"source","obj":"Allie"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"Allie","color":"#ecc693","default":true}]}]}}