http://purl.uniprot.org/citations/30107486 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/30107486 | http://www.w3.org/2000/01/rdf-schema#comment | "The B-cell response to antigen is critically regulated by co-receptors. CD21 (complement receptor 2) amplifies the response to antigen linked to its ligands, specific C3 fragments. In contrast, human Fc receptor-like 5 (FCRL5), a novel IgG receptor, was reported to inhibit B-cell receptor (BCR) signaling. Here, we show that CD21 and FCRL5 physically associate, suggesting that immune complexes containing both C3 fragment and IgG could simultaneously engage the pre-assembled receptors. We found that activating signaling molecules such as CD19, active PLCγ2 and BTK were rapidly recruited to FCRL5 upon engagement, suggesting a novel activating function for FCRL5. We confirmed that FCRL5 through its ITIMs (immunoreceptor tyrosine-based inhibitory motif) inhibited BCR signaling in the absence of CD21 stimulation. In contrast, triple engagement of FCRL5, CD21 and the BCR led to a superior calcium response compared to CD21 and BCR co-stimulation, in both cell lines and tonsil B cells. Furthermore, the novel activating function was independent of established FCRL5 signaling motifs. While human peripheral B cells express either FCRL5 or CD21, we identified a sizable subset of tonsil B cells which co-express the two receptors. We propose that FCRL5 has dual signaling capacity, while CD21 co-engagement serves as molecular switch, converting FCRL5 from a negative to a positive co-receptor. In tissues, B cells that co-express FCRL5 and CD21 could robustly respond to IgG immune complexes loaded with C3 fragments."xsd:string |
http://purl.uniprot.org/citations/30107486 | http://purl.org/dc/terms/identifier | "doi:10.1093/intimm/dxy052"xsd:string |
http://purl.uniprot.org/citations/30107486 | http://purl.uniprot.org/core/author | "Li H."xsd:string |
http://purl.uniprot.org/citations/30107486 | http://purl.uniprot.org/core/author | "Franco A."xsd:string |
http://purl.uniprot.org/citations/30107486 | http://purl.uniprot.org/core/author | "Tolnay M."xsd:string |
http://purl.uniprot.org/citations/30107486 | http://purl.uniprot.org/core/author | "Dement-Brown J."xsd:string |
http://purl.uniprot.org/citations/30107486 | http://purl.uniprot.org/core/author | "Kraus Z."xsd:string |
http://purl.uniprot.org/citations/30107486 | http://purl.uniprot.org/core/author | "Seibert N."xsd:string |
http://purl.uniprot.org/citations/30107486 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
http://purl.uniprot.org/citations/30107486 | http://purl.uniprot.org/core/name | "Int Immunol"xsd:string |
http://purl.uniprot.org/citations/30107486 | http://purl.uniprot.org/core/pages | "569-578"xsd:string |
http://purl.uniprot.org/citations/30107486 | http://purl.uniprot.org/core/title | "CD21 and FCRL5 form a receptor complex with robust B-cell activating capacity."xsd:string |
http://purl.uniprot.org/citations/30107486 | http://purl.uniprot.org/core/volume | "30"xsd:string |
http://purl.uniprot.org/citations/30107486 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/30107486 |
http://purl.uniprot.org/citations/30107486 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/30107486 |
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http://purl.uniprot.org/uniprot/#_Q08578-mappedCitation-30107486 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/30107486 |
http://purl.uniprot.org/uniprot/#_Q9H2B3-mappedCitation-30107486 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/30107486 |
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