期刊
JOURNAL OF IMMUNOLOGY
卷 193, 期 7, 页码 3257-3261出版社
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.1301886
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资金
- National Institutes of Health [P01-AR050256]
- Deutsche Forschungsgemeinschaft [HO2209/1-1]
Sensing of nucleic acids by TLRs is crucial in the host defense against viruses and bacteria. Unc-93 homolog B1 (UNC93B1) regulates the trafficking of nucleic acid-sensing TLRs from the endoplasmic reticulum to endolysosomes, where the TLRs encounter their respective ligands and become activated. In this article, we show that a carboxyl-terminal tyrosine-based sorting motif (Yxx Phi) in UNC93B1 differentially regulates human nucleic acid-sensing TLRs in a receptor-and ligand-specific manner. Destruction of YxxF abolished TLR7, TLR8, and TLR9 activity toward nucleic acids in human B cells and monocytes, whereas TLR8 responses toward small molecules remained intact. YxxF in UNC93B1 influenced the subcellular localization of human UNC93B1 via both adapter protein complex (AP)1- and AP2-dependent trafficking pathways. However, loss of AP function was not causal for altered TLR responses, suggesting AP-independent functions of YxxF in UNC93B1.
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