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A role for the adaptor proteins TRAM and TRIF in toll-like receptor 2 signaling

Nilsen, Nadra; Gregory I., Vladimer; Stenvik, Jørgen; Ørning, Mathias Pontus; Zeid-Kilani, Maria Vanessa; Bugge, Marit; Bergstrøm, Bjarte; Conlon, Joseph; Husebye, Harald; Amy, Hise; Fitzgerald, Katherine A.; Espevik, Terje; Lien, Egil
Journal article, Peer reviewed
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URI
http://hdl.handle.net/11250/2458403
Date
2015
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  • Institutt for klinisk og molekylær medisin [2120]
  • Publikasjoner fra CRIStin - NTNU [21889]
Original version
Journal of Biological Chemistry. 2015, 290 (6), 3209-3222.   10.1074/jbc.M114.593426
Abstract
Toll-like receptors (TLRs) are involved in sensing invading microbes by host innate immunity. TLR2 recognizes bacterial lipoproteins/lipopeptides, and lipopolysaccharide activates TLR4. TLR2 and TLR4 signal via the Toll/interleukin-1 receptor adaptors MyD88 and MAL, leading to NF-κB activation. TLR4 also utilizes the adaptors TRAM and TRIF, resulting in activation of interferon regulatory factor (IRF) 3. Here, we report a new role for TRAM and TRIF in TLR2 regulation and signaling. Interestingly, we observed that TLR2-mediated induction of the chemokine Ccl5 was impaired in TRAM or TRIF deficient macrophages. Inhibition of endocytosis reduced Ccl5 release, and the data also suggested that TRAM and TLR2 co-localize in early endosomes, supporting the hypothesis that signaling may occur from an intracellular compartment. Ccl5 release following lipoprotein challenge additionally involved the kinase Tbk-1 and Irf3, as well as MyD88 and Irf1. Induction of Interferon-β and Ccl4 by lipoproteins was also partially impaired in cells lacking TRIF cells. Our results show a novel function of TRAM and TRIF in TLR2-mediated signal transduction, and the findings broaden our understanding of how Toll/interleukin-1 receptor adaptor proteins may participate in signaling downstream from TLR2.
Publisher
American Society for Biochemistry and Molecular Biology
Journal
Journal of Biological Chemistry

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