The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Poly(dI·dC)-induced Toll-like Receptor 3 (TLR3)-mediated Activation of NFκB and MAP Kinase Is through an Interleukin-1 Receptor-associated Kinase (IRAK)-independent Pathway Employing the Signaling Components TLR3-TRAF6-TAK1-TAB2-PKR
Open accessAbstract
Recent studies show that a member of the interleukin-1 (IL-1)/Toll receptor superfamily, Toll-like receptor 3 (TLR3), recognizes double-stranded RNA (dsRNA). Because of the similarity in their cytoplasmic domains, IL-1/Toll receptors share signaling components that associate with the IL-1 receptor, including IL-1 receptor-associated kinase (IRAK), MyD88, and TRAF6. However, we find that, in response to dsRNA, TLR3 can mediate the activation of both NFkappaB and mitogen-activated protein (MAP) kinases in IL-1-unresponsive mutant cell lines, including IRAK-deficient I1A and I3A cells, which are defective in a component that is downstream of IL-1R but upstream of IRAK. These results clearly indicate that TLR3 does not simply share the signaling components employed by the IL-1 receptor. Through biochemical analyses we have identified an IRAK-independent TLR3-mediated pathway. Upon binding of dsRNA to TLR3, TRAF6, TAK1, and TAB2 are recruited to the receptor to form a complex, which then translocates to the cytosol where TAK1 is phosphorylated and activated. The dsRNA-dependent protein kinase (PKR) is also detected in this signal-induced TAK1 complex. Kinase inactive mutants of TAK1 (TAK1DN) and PKR (PKRDN) inhibit poly(dI.dC)-induced TLR3-mediated NFkappaB activation, suggesting that both of these kinases play important roles in this pathway.
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A Toll-like receptor recognizes bacterial DNA
Hemmi, H., Takeuchi, O., Kawai, T., Kaisho, T., Sato, S., Sanjo, H., Matsumoto, M., Hoshino, K., Wagner, H., Takeda, K., et al. (2000) · Nature · doi:10.1038/35047123 · Cited by 6,491
Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3
Alexopoulou, L., Holt, A. C., Medzhitov, R., & Flavell, R. A. (2001) · Nature · doi:10.1038/35099560 · Cited by 6,129
Toll-like receptors: critical proteins linking innate and acquired immunity
Akira, S., Takeda, K., & Kaisho, T. (2001) · Nature Immunology · doi:10.1038/90609 · Cited by 4,777
Kessler, D. S., Veals, S. A., Fu, X. Y., & Levy, D. E. (1990) · Genes & Development · doi:10.1101/gad.4.10.1753 · Cited by 312
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Signal transduction by the lipopolysaccharide receptor, Toll-like receptor-4
Pålsson‐McDermott, E. M., & O'Neill, L. A. J. (2004) · Immunology · doi:10.1111/j.1365-2567.2004.01976.x · Cited by 1,254
Impact of Protein Kinase PKR in Cell Biology: from Antiviral to Antiproliferative Action
García, M. A., Gil, J., Ventoso, I., Guerra, S., Domingo, E., Rivas, C., & Esteban, M. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00027-06 · Cited by 818
The dsRNA protein kinase PKR: Virus and cell control
García, M. A., Meurs, E. F., & Esteban, M. (2007) · Biochimie · doi:10.1016/j.biochi.2007.03.001 · Cited by 644
The interferon regulatory factor, IRF5, is a central mediator of toll-like receptor 7 signaling
Schoenemeyer, A., Barnes, B. J., Mancl, M. E., Latz, E., Goutagny, N., Pitha, P. M., Fitzgerald, K. A., & Golenbock, D. T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412584200 · Cited by 411
Cunningham, C., Campion, S., Teeling, J., Felton, L., & Perry, V. H. (2007) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2006.12.007 · Cited by 318
p53 regulates Toll-like receptor 3 expression and function in human epithelial cell lines
Taura, M., Eguma, A., Suico, M. A., Shuto, T., Koga, T., Komatsu, K., Komune, T., Sato, T., Saya, H., Li, J.-D., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01202-08 · Cited by 129
Toll-like receptors in skin infections and inflammatory diseases
Lai, Y., & Gallo, R. (2008) · Infectious Disorders - Drug Targets · doi:10.2174/1871526510808030144 · Cited by 119
Bonnet, M. C., Daurat, C., Ottone, C., & Meurs, E. F. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.02.010 · Cited by 71
Salerno, F., Howden, A. J. M., Matheson, L. S., Gizlenci, Ö., Screen, M., Lingel, H., Brunner-Weinzierl, M. C., & Turner, M. (2023) · Nature Communications · doi:10.1038/s41467-023-40621-2 · Cited by 29
Metadata
- Authors
- Jiang, Z., Zamanian-Daryoush, M., Nie, H., Silva, A. M., Williams, B. R. G., & Li, X.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-05
- Volume
- 278
- Issue
- 19
- Pages
- 16713-16719
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1972327788
- Cited by
- 297
- References
- 4
- FWCI
- 10.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
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