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http://purl.uniprot.org/citations/31328160http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31328160http://www.w3.org/2000/01/rdf-schema#comment"B cell activation is regulated by the stimulatory or inhibitory co-receptors of B cell receptors (BCRs). Here, we investigated the signaling mechanism of Fc receptor-like 1 (FcRL1), a newly identified BCR co-receptor. FcRL1 was passively recruited into B cell immunological synapses upon BCR engagement in the absence of FcRL1 cross-linking, suggesting that FcRL1 may intrinsically regulate B cell activation and function. BCR cross-linking alone led to the phosphorylation of the intracellular Y281ENV motif of FcRL1 to provide a docking site for c-Abl, an SH2 domain-containing kinase. The FcRL1 and c-Abl signaling module, in turn, potently augmented B cell activation and proliferation. FcRL1-deficient mice exhibited markedly impaired formation of extrafollicular plasmablasts and germinal centers, along with decreased antibody production upon antigen stimulation. These findings reveal a critical BCR signal-enhancing function of FcRL1 through its intrinsic recruitment to B cell immunological synapses and subsequent recruitment of c-Abl upon BCR cross-linking."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.org/dc/terms/identifier"doi:10.1126/sciadv.aaw0315"xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/author"Liu W."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/author"Kim T.J."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/author"Zhao M."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/author"Wang F."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/author"Yang Z."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/author"Zhao X."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/author"Wu C."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/author"Yi J."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/author"Xie H."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/author"Li Q.Z."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/author"Ahsan A."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/author"Raman I."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/name"Sci Adv"xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/pages"eaaw0315"xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/title"Fc receptor-like 1 intrinsically recruits c-Abl to enhance B cell activation and function."xsd:string
http://purl.uniprot.org/citations/31328160http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/31328160http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31328160
http://purl.uniprot.org/citations/31328160http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31328160
http://purl.uniprot.org/uniprot/#_A0A0A6YVY6-mappedCitation-31328160http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31328160
http://purl.uniprot.org/uniprot/#_A0A0A6YXB2-mappedCitation-31328160http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31328160