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Volumn 18, Issue 1, 2017, Pages 6-17

Microbe-inducible trafficking pathways that control Toll-like receptor signaling

Author keywords

innate immunity; membrane trafficking; organelles; signal transduction; SMOCs; TAXI proteins; Toll like receptors

Indexed keywords

ADAPTOR PROTEIN; PROTEIN; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 1; TOLL LIKE RECEPTOR 10; TOLL LIKE RECEPTOR 11; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 5; TOLL LIKE RECEPTOR 6; TOLL LIKE RECEPTOR 7; TOLL LIKE RECEPTOR 8; TOLL LIKE RECEPTOR 9; TRANSPORTER ASSOCIATED WITH THE EXECUTION OF INFLAMMATION PROTEIN; UNCLASSIFIED DRUG; LIGAND;

EID: 85006632183     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/tra.12454     Document Type: Review
Times cited : (24)

References (116)
  • 1
    • 84927639135 scopus 로고    scopus 로고
    • Innate immune pattern recognition: a cell biological perspective
    • Brubaker SW, Bonham KS, Zanoni I, Kagan JC. Innate immune pattern recognition: a cell biological perspective. Annu Rev Immunol. 2015;33:257-290.
    • (2015) Annu Rev Immunol , vol.33 , pp. 257-290
    • Brubaker, S.W.1    Bonham, K.S.2    Zanoni, I.3    Kagan, J.C.4
  • 2
    • 84879330799 scopus 로고    scopus 로고
    • Innate immune recognition of the microbiota promotes host-microbial symbiosis
    • Chu H, Mazmanian SK. Innate immune recognition of the microbiota promotes host-microbial symbiosis. Nat Immunol. 2013;14(7):668-675.
    • (2013) Nat Immunol , vol.14 , Issue.7 , pp. 668-675
    • Chu, H.1    Mazmanian, S.K.2
  • 3
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway CA Jr. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb Symp Quant Biol. 1989;54(Pt 1):1-13.
    • (1989) Cold Spring Harb Symp Quant Biol , vol.54 , pp. 1-13
    • Janeway, C.A.1
  • 4
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi O, Akira S. Pattern recognition receptors and inflammation. Cell. 2010;140(6):805-820.
    • (2010) Cell , vol.140 , Issue.6 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 5
    • 67651091732 scopus 로고    scopus 로고
    • Patterns of pathogenesis: discrimination of pathogenic and nonpathogenic microbes by the innate immune system
    • Vance RE, Isberg RR, Portnoy DA. Patterns of pathogenesis: discrimination of pathogenic and nonpathogenic microbes by the innate immune system. Cell Host Microbe. 2009;6(1):10-21.
    • (2009) Cell Host Microbe , vol.6 , Issue.1 , pp. 10-21
    • Vance, R.E.1    Isberg, R.R.2    Portnoy, D.A.3
  • 6
    • 66949122854 scopus 로고    scopus 로고
    • Approaching the asymptote: 20 years later
    • Medzhitov R. Approaching the asymptote: 20 years later. Immunity. 2009;30(6):766-775.
    • (2009) Immunity , vol.30 , Issue.6 , pp. 766-775
    • Medzhitov, R.1
  • 7
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov R, Preston-Hurlburt P, Janeway CA Jr. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature. 1997;388(6640):394-397.
    • (1997) Nature , vol.388 , Issue.6640 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway, C.A.3
  • 8
    • 0032509295 scopus 로고    scopus 로고
    • Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene
    • Poltorak A, He X, Smirnova I, et al. Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science. 1998;282(5396):2085-2088.
    • (1998) Science , vol.282 , Issue.5396 , pp. 2085-2088
    • Poltorak, A.1    He, X.2    Smirnova, I.3
  • 9
    • 58049203835 scopus 로고    scopus 로고
    • Systems biology of innate immunity
    • Zak DE, Aderem A. Systems biology of innate immunity. Immunol Rev. 2009;227(1):264-282.
    • (2009) Immunol Rev , vol.227 , Issue.1 , pp. 264-282
    • Zak, D.E.1    Aderem, A.2
  • 10
    • 84859985764 scopus 로고    scopus 로고
    • Phosphoinositide binding by the Toll adaptor dMyD88 controls antibacterial responses in Drosophila
    • Marek LR, Kagan JC. Phosphoinositide binding by the Toll adaptor dMyD88 controls antibacterial responses in Drosophila. Immunity. 2012;36(4):612-622.
    • (2012) Immunity , vol.36 , Issue.4 , pp. 612-622
    • Marek, L.R.1    Kagan, J.C.2
  • 11
    • 68849085894 scopus 로고    scopus 로고
    • A cell biological view of Toll-like receptor function: regulation through compartmentalization
    • Barton GM, Kagan JC. A cell biological view of Toll-like receptor function: regulation through compartmentalization. Nat Rev Immunol. 2009;9(8):535-542.
    • (2009) Nat Rev Immunol , vol.9 , Issue.8 , pp. 535-542
    • Barton, G.M.1    Kagan, J.C.2
  • 12
    • 33750369226 scopus 로고    scopus 로고
    • Toll-like receptors in systemic autoimmune disease
    • Marshak-Rothstein A. Toll-like receptors in systemic autoimmune disease. Nat Rev Immunol. 2006;6(11):823-835.
    • (2006) Nat Rev Immunol , vol.6 , Issue.11 , pp. 823-835
    • Marshak-Rothstein, A.1
  • 13
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors
    • Kawai T, Akira S. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat Immunol. 2010;11(5):373-384.
    • (2010) Nat Immunol , vol.11 , Issue.5 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 14
    • 0033120081 scopus 로고    scopus 로고
    • Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: evidence for TLR4 as the Lps gene product
    • Hoshino K, Takeuchi O, Kawai T, et al. Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: evidence for TLR4 as the Lps gene product. J Immunol. 1999;162(7):3749-3752.
    • (1999) J Immunol , vol.162 , Issue.7 , pp. 3749-3752
    • Hoshino, K.1    Takeuchi, O.2    Kawai, T.3
  • 15
    • 0037153130 scopus 로고    scopus 로고
    • The adaptor molecule TIRAP provides signalling specificity for Toll-like receptors
    • Horng T, Barton GM, Flavell RA, Medzhitov R. The adaptor molecule TIRAP provides signalling specificity for Toll-like receptors. Nature. 2002;420(6913):329-333.
    • (2002) Nature , vol.420 , Issue.6913 , pp. 329-333
    • Horng, T.1    Barton, G.M.2    Flavell, R.A.3    Medzhitov, R.4
  • 16
    • 0037153191 scopus 로고    scopus 로고
    • Essential role for TIRAP in activation of the signalling cascade shared by TLR2 and TLR4
    • Yamamoto M, Sato S, Hemmi H, et al. Essential role for TIRAP in activation of the signalling cascade shared by TLR2 and TLR4. Nature. 2002;420(6913):324-329.
    • (2002) Nature , vol.420 , Issue.6913 , pp. 324-329
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3
  • 17
    • 0043176281 scopus 로고    scopus 로고
    • Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway
    • Yamamoto M, Sato S, Hemmi H, et al. Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway. Science. 2003;301(5633):640-643.
    • (2003) Science , vol.301 , Issue.5633 , pp. 640-643
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3
  • 18
    • 0242624622 scopus 로고    scopus 로고
    • TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway
    • Yamamoto M, Sato S, Hemmi H, et al. TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway. Nat Immunol. 2003;4(11):1144-1150.
    • (2003) Nat Immunol , vol.4 , Issue.11 , pp. 1144-1150
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3
  • 19
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4
    • Shimazu R, Akashi S, Ogata H, et al. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J Exp Med. 1999;189(11):1777-1782.
    • (1999) J Exp Med , vol.189 , Issue.11 , pp. 1777-1782
    • Shimazu, R.1    Akashi, S.2    Ogata, H.3
  • 20
    • 34548222514 scopus 로고    scopus 로고
    • Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran
    • Kim HM, Park BS, Kim JI, et al. Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Cell. 2007;130(5):906-917.
    • (2007) Cell , vol.130 , Issue.5 , pp. 906-917
    • Kim, H.M.1    Park, B.S.2    Kim, J.I.3
  • 21
    • 35048817885 scopus 로고    scopus 로고
    • Kinetics of binding of LPS to recombinant CD14, TLR4, and MD-2 proteins
    • Shin HJ, Lee H, Park JD, et al. Kinetics of binding of LPS to recombinant CD14, TLR4, and MD-2 proteins. Mol Cells. 2007;24(1):124-119.
    • (2007) Mol Cells , vol.24 , Issue.1 , pp. 119-124
    • Shin, H.J.1    Lee, H.2    Park, J.D.3
  • 22
    • 0022462376 scopus 로고
    • Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit serum
    • Tobias PS, Soldau K, Ulevitch RJ. Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit serum. J Exp Med. 1986;164(3):777-793.
    • (1986) J Exp Med , vol.164 , Issue.3 , pp. 777-793
    • Tobias, P.S.1    Soldau, K.2    Ulevitch, R.J.3
  • 23
    • 0025166114 scopus 로고
    • CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein
    • Wright SD, Ramos RA, Tobias PS, Ulevitch RJ, Mathison JC. CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein. Science. 1990;249(4975):1431-1433.
    • (1990) Science , vol.249 , Issue.4975 , pp. 1431-1433
    • Wright, S.D.1    Ramos, R.A.2    Tobias, P.S.3    Ulevitch, R.J.4    Mathison, J.C.5
  • 24
    • 84899137757 scopus 로고    scopus 로고
    • A cross-disciplinary perspective on the innate immune responses to bacterial lipopolysaccharide
    • Tan Y, Kagan JC. A cross-disciplinary perspective on the innate immune responses to bacterial lipopolysaccharide. Mol Cell. 2014;54(2):212-223.
    • (2014) Mol Cell , vol.54 , Issue.2 , pp. 212-223
    • Tan, Y.1    Kagan, J.C.2
  • 25
    • 35348856289 scopus 로고    scopus 로고
    • Regulation of interactions of Gram-negative bacterial endotoxins with mammalian cells
    • Gioannini TL, Weiss JP. Regulation of interactions of Gram-negative bacterial endotoxins with mammalian cells. Immunol Res. 2007;39(1-3):249-260.
    • (2007) Immunol Res , vol.39 , Issue.1-3 , pp. 249-260
    • Gioannini, T.L.1    Weiss, J.P.2
  • 26
    • 0037096172 scopus 로고    scopus 로고
    • Mediators of innate immune recognition of bacteria concentrate in lipid rafts and facilitate lipopolysaccharide-induced cell activation
    • Triantafilou M, Miyake K, Golenbock DT, Triantafilou K. Mediators of innate immune recognition of bacteria concentrate in lipid rafts and facilitate lipopolysaccharide-induced cell activation. J Cell Sci. 2002;115(Pt 12):2603-2611.
    • (2002) J Cell Sci , vol.115 , pp. 2603-2611
    • Triantafilou, M.1    Miyake, K.2    Golenbock, D.T.3    Triantafilou, K.4
  • 27
    • 84892663982 scopus 로고    scopus 로고
    • The small GTPase Arf6 is essential for the Tram/Trif pathway in TLR4 signaling
    • Van Acker T, Eyckerman S, Vande Walle L, et al. The small GTPase Arf6 is essential for the Tram/Trif pathway in TLR4 signaling. J Biol Chem. 2014;289(3):1364-1376.
    • (2014) J Biol Chem , vol.289 , Issue.3 , pp. 1364-1376
    • Van Acker, T.1    Eyckerman, S.2    Vande Walle, L.3
  • 29
    • 81055129630 scopus 로고    scopus 로고
    • CD14 controls the LPS-induced endocytosis of Toll-like receptor 4
    • Zanoni I, Ostuni R, Marek LR, et al. CD14 controls the LPS-induced endocytosis of Toll-like receptor 4. Cell. 2011;147(4):868-880.
    • (2011) Cell , vol.147 , Issue.4 , pp. 868-880
    • Zanoni, I.1    Ostuni, R.2    Marek, L.R.3
  • 30
    • 0033952703 scopus 로고    scopus 로고
    • Tlr4: central component of the sole mammalian LPS sensor
    • Beutler B. Tlr4: central component of the sole mammalian LPS sensor. Curr Opin Immunol. 2000;12(1):20-26.
    • (2000) Curr Opin Immunol , vol.12 , Issue.1 , pp. 20-26
    • Beutler, B.1
  • 31
    • 80455176839 scopus 로고    scopus 로고
    • Non-canonical inflammasome activation targets caspase-11
    • Kayagaki N, Warming S, Lamkanfi M, et al. Non-canonical inflammasome activation targets caspase-11. Nature. 2011;479(7371):117-121.
    • (2011) Nature , vol.479 , Issue.7371 , pp. 117-121
    • Kayagaki, N.1    Warming, S.2    Lamkanfi, M.3
  • 32
    • 84883790050 scopus 로고    scopus 로고
    • Cytoplasmic LPS activates caspase-11: implications in TLR4-independent endotoxic shock
    • Hagar JA, Powell DA, Aachoui Y, Ernst RK, Miao EA. Cytoplasmic LPS activates caspase-11: implications in TLR4-independent endotoxic shock. Science. 2013;341(6151):1250-1253.
    • (2013) Science , vol.341 , Issue.6151 , pp. 1250-1253
    • Hagar, J.A.1    Powell, D.A.2    Aachoui, Y.3    Ernst, R.K.4    Miao, E.A.5
  • 33
    • 84947428414 scopus 로고    scopus 로고
    • Mechanisms of Toll-like receptor 4 endocytosis reveal a common immune-evasion strategy used by pathogenic and commensal bacteria
    • Tan Y, Zanoni I, Cullen TW, Goodman AL, Kagan JC. Mechanisms of Toll-like receptor 4 endocytosis reveal a common immune-evasion strategy used by pathogenic and commensal bacteria. Immunity. 2015;43(5):909-922.
    • (2015) Immunity , vol.43 , Issue.5 , pp. 909-922
    • Tan, Y.1    Zanoni, I.2    Cullen, T.W.3    Goodman, A.L.4    Kagan, J.C.5
  • 34
    • 84856745386 scopus 로고    scopus 로고
    • Phospholipase Cgamma-2 and intracellular calcium are required for lipopolysaccharide-induced Toll-like receptor 4 (TLR4) endocytosis and interferon regulatory factor 3 (IRF3) activation
    • Chiang CY, Veckman V, Limmer K, David M. Phospholipase Cgamma-2 and intracellular calcium are required for lipopolysaccharide-induced Toll-like receptor 4 (TLR4) endocytosis and interferon regulatory factor 3 (IRF3) activation. J Biol Chem. 2012;287(6):3704-3709.
    • (2012) J Biol Chem , vol.287 , Issue.6 , pp. 3704-3709
    • Chiang, C.Y.1    Veckman, V.2    Limmer, K.3    David, M.4
  • 35
    • 27144521657 scopus 로고    scopus 로고
    • Dectin-1 activates Syk tyrosine kinase in a dynamic subset of macrophages for reactive oxygen production
    • Underhill DM, Rossnagle E, Lowell CA, Simmons RM. Dectin-1 activates Syk tyrosine kinase in a dynamic subset of macrophages for reactive oxygen production. Blood. 2005;106(7):2543-2550.
    • (2005) Blood , vol.106 , Issue.7 , pp. 2543-2550
    • Underhill, D.M.1    Rossnagle, E.2    Lowell, C.A.3    Simmons, R.M.4
  • 36
    • 20244363662 scopus 로고    scopus 로고
    • Syk-dependent cytokine induction by Dectin-1 reveals a novel pattern recognition pathway for C type lectins
    • Rogers NC, Slack EC, Edwards AD, et al. Syk-dependent cytokine induction by Dectin-1 reveals a novel pattern recognition pathway for C type lectins. Immunity. 2005;22(4):507-517.
    • (2005) Immunity , vol.22 , Issue.4 , pp. 507-517
    • Rogers, N.C.1    Slack, E.C.2    Edwards, A.D.3
  • 37
    • 0030829551 scopus 로고    scopus 로고
    • A critical role for Syk in signal transduction and phagocytosis mediated by Fcgamma receptors on macrophages
    • Crowley MT, Costello PS, Fitzer-Attas CJ, et al. A critical role for Syk in signal transduction and phagocytosis mediated by Fcgamma receptors on macrophages. J Exp Med. 1997;186(7):1027-1039.
    • (1997) J Exp Med , vol.186 , Issue.7 , pp. 1027-1039
    • Crowley, M.T.1    Costello, P.S.2    Fitzer-Attas, C.J.3
  • 38
    • 79960720320 scopus 로고    scopus 로고
    • Molecular mechanism and physiological functions of clathrin-mediated endocytosis
    • McMahon HT, Boucrot E. Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nat Rev Mol Cell Biol. 2011;12(8):517-533.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , Issue.8 , pp. 517-533
    • McMahon, H.T.1    Boucrot, E.2
  • 39
    • 34250813748 scopus 로고    scopus 로고
    • Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa
    • Ohto U, Fukase K, Miyake K, Satow Y. Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa. Science. 2007;316(5831):1632-1634.
    • (2007) Science , vol.316 , Issue.5831 , pp. 1632-1634
    • Ohto, U.1    Fukase, K.2    Miyake, K.3    Satow, Y.4
  • 40
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex
    • Park BS, Song DH, Kim HM, Choi BS, Lee H, Lee JO. The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature. 2009;458(7242):1191-1195.
    • (2009) Nature , vol.458 , Issue.7242 , pp. 1191-1195
    • Park, B.S.1    Song, D.H.2    Kim, H.M.3    Choi, B.S.4    Lee, H.5    Lee, J.O.6
  • 41
    • 15744396047 scopus 로고    scopus 로고
    • Crystal structure of CD14 and its implications for lipopolysaccharide signaling
    • Kim JI, Lee CJ, Jin MS, et al. Crystal structure of CD14 and its implications for lipopolysaccharide signaling. J Biol Chem. 2005;280(12):11347-11351.
    • (2005) J Biol Chem , vol.280 , Issue.12 , pp. 11347-11351
    • Kim, J.I.1    Lee, C.J.2    Jin, M.S.3
  • 42
    • 77958487596 scopus 로고    scopus 로고
    • The Rab11a GTPase controls Toll-like receptor 4-induced activation of interferon regulatory factor-3 on phagosomes
    • Husebye H, Aune MH, Stenvik J, et al. The Rab11a GTPase controls Toll-like receptor 4-induced activation of interferon regulatory factor-3 on phagosomes. Immunity. 2010;33(4):583-596.
    • (2010) Immunity , vol.33 , Issue.4 , pp. 583-596
    • Husebye, H.1    Aune, M.H.2    Stenvik, J.3
  • 43
    • 40949134086 scopus 로고    scopus 로고
    • TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-beta
    • Kagan JC, Su T, Horng T, Chow A, Akira S, Medzhitov R. TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-beta. Nat Immunol. 2008;9(4):361-368.
    • (2008) Nat Immunol , vol.9 , Issue.4 , pp. 361-368
    • Kagan, J.C.1    Su, T.2    Horng, T.3    Chow, A.4    Akira, S.5    Medzhitov, R.6
  • 44
    • 84905402595 scopus 로고    scopus 로고
    • TLR signals induce phagosomal MHC-I delivery from the endosomal recycling compartment to allow cross-presentation
    • Nair-Gupta P, Baccarini A, Tung N, et al. TLR signals induce phagosomal MHC-I delivery from the endosomal recycling compartment to allow cross-presentation. Cell. 2014;158(3):506-521.
    • (2014) Cell , vol.158 , Issue.3 , pp. 506-521
    • Nair-Gupta, P.1    Baccarini, A.2    Tung, N.3
  • 46
    • 33644508366 scopus 로고    scopus 로고
    • Endocytic pathways regulate Toll-like receptor 4 signaling and link innate and adaptive immunity
    • Husebye H, Halaas O, Stenmark H, et al. Endocytic pathways regulate Toll-like receptor 4 signaling and link innate and adaptive immunity. EMBO J. 2006;25(4):683-692.
    • (2006) EMBO J , vol.25 , Issue.4 , pp. 683-692
    • Husebye, H.1    Halaas, O.2    Stenmark, H.3
  • 47
    • 84861459238 scopus 로고    scopus 로고
    • Adaptor protein-3 in dendritic cells facilitates phagosomal toll-like receptor signaling and antigen presentation to CD4(+) T cells
    • Mantegazza AR, Guttentag SH, El-Benna J, et al. Adaptor protein-3 in dendritic cells facilitates phagosomal toll-like receptor signaling and antigen presentation to CD4(+) T cells. Immunity. 2012;36(5):782-794.
    • (2012) Immunity , vol.36 , Issue.5 , pp. 782-794
    • Mantegazza, A.R.1    Guttentag, S.H.2    El-Benna, J.3
  • 48
    • 77956358594 scopus 로고    scopus 로고
    • Ras-related protein Rab10 facilitates TLR4 signaling by promoting replenishment of TLR4 onto the plasma membrane
    • Wang D, Lou J, Ouyang C, et al. Ras-related protein Rab10 facilitates TLR4 signaling by promoting replenishment of TLR4 onto the plasma membrane. Proc Natl Acad Sci USA. 2010;107(31):13806-13811.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.31 , pp. 13806-13811
    • Wang, D.1    Lou, J.2    Ouyang, C.3
  • 49
    • 0034610291 scopus 로고    scopus 로고
    • The repertoire for pattern recognition of pathogens by the innate immune system is defined by cooperation between toll-like receptors
    • Ozinsky A, Underhill DM, Fontenot JD, et al. The repertoire for pattern recognition of pathogens by the innate immune system is defined by cooperation between toll-like receptors. Proc Natl Acad Sci USA. 2000;97(25):13766-13771.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.25 , pp. 13766-13771
    • Ozinsky, A.1    Underhill, D.M.2    Fontenot, J.D.3
  • 50
    • 38749153572 scopus 로고    scopus 로고
    • Mannose-binding lectin enhances Toll-like receptors 2 and 6 signaling from the phagosome
    • Ip WK, Takahashi K, Moore KJ, Stuart LM, Ezekowitz RA. Mannose-binding lectin enhances Toll-like receptors 2 and 6 signaling from the phagosome. J Exp Med. 2008;205(1):169-181.
    • (2008) J Exp Med , vol.205 , Issue.1 , pp. 169-181
    • Ip, W.K.1    Takahashi, K.2    Moore, K.J.3    Stuart, L.M.4    Ezekowitz, R.A.5
  • 51
    • 15844428423 scopus 로고    scopus 로고
    • Binding of lipopeptide to CD14 induces physical proximity of CD14, TLR2 and TLR1
    • Manukyan M, Triantafilou K, Triantafilou M, et al. Binding of lipopeptide to CD14 induces physical proximity of CD14, TLR2 and TLR1. Eur J Immunol. 2005;35(3):911-921.
    • (2005) Eur J Immunol , vol.35 , Issue.3 , pp. 911-921
    • Manukyan, M.1    Triantafilou, K.2    Triantafilou, M.3
  • 52
    • 13444280215 scopus 로고    scopus 로고
    • CD36 is a sensor of diacylglycerides
    • Hoebe K, Georgel P, Rutschmann S, et al. CD36 is a sensor of diacylglycerides. Nature. 2005;433(7025):523-527.
    • (2005) Nature , vol.433 , Issue.7025 , pp. 523-527
    • Hoebe, K.1    Georgel, P.2    Rutschmann, S.3
  • 53
    • 34548608447 scopus 로고    scopus 로고
    • Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide
    • Jin MS, Kim SE, Heo JY, et al. Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide. Cell. 2007;130(6):1071-1082.
    • (2007) Cell , vol.130 , Issue.6 , pp. 1071-1082
    • Jin, M.S.1    Kim, S.E.2    Heo, J.Y.3
  • 54
    • 71749118913 scopus 로고    scopus 로고
    • Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer
    • Kang JY, Nan X, Jin MS, et al. Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer. Immunity. 2009;31(6):873-884.
    • (2009) Immunity , vol.31 , Issue.6 , pp. 873-884
    • Kang, J.Y.1    Nan, X.2    Jin, M.S.3
  • 55
    • 33750070631 scopus 로고    scopus 로고
    • Membrane sorting of toll-like receptor (TLR)-2/6 and TLR2/1 heterodimers at the cell surface determines heterotypic associations with CD36 and intracellular targeting
    • Triantafilou M, Gamper FG, Haston RM, et al. Membrane sorting of toll-like receptor (TLR)-2/6 and TLR2/1 heterodimers at the cell surface determines heterotypic associations with CD36 and intracellular targeting. J Biol Chem. 2006;281(41):31002-31011.
    • (2006) J Biol Chem , vol.281 , Issue.41 , pp. 31002-31011
    • Triantafilou, M.1    Gamper, F.G.2    Haston, R.M.3
  • 56
    • 23744514918 scopus 로고    scopus 로고
    • Response to Staphylococcus aureus requires CD36-mediated phagocytosis triggered by the COOH-terminal cytoplasmic domain
    • Stuart LM, Deng J, Silver JM, et al. Response to Staphylococcus aureus requires CD36-mediated phagocytosis triggered by the COOH-terminal cytoplasmic domain. J Cell Biol. 2005;170(3):477-485.
    • (2005) J Cell Biol , vol.170 , Issue.3 , pp. 477-485
    • Stuart, L.M.1    Deng, J.2    Silver, J.M.3
  • 57
    • 84875368795 scopus 로고    scopus 로고
    • Multimolecular signaling complexes enable Syk-mediated signaling of CD36 internalization
    • Heit B, Kim H, Cosio G, et al. Multimolecular signaling complexes enable Syk-mediated signaling of CD36 internalization. Dev Cell. 2013;24(4):372-383.
    • (2013) Dev Cell , vol.24 , Issue.4 , pp. 372-383
    • Heit, B.1    Kim, H.2    Cosio, G.3
  • 58
    • 0029809772 scopus 로고    scopus 로고
    • CD36 is palmitoylated on both N- and C-terminal cytoplasmic tails
    • Tao N, Wagner SJ, Lublin DM. CD36 is palmitoylated on both N- and C-terminal cytoplasmic tails. J Biol Chem. 1996;271(37):22315-22320.
    • (1996) J Biol Chem , vol.271 , Issue.37 , pp. 22315-22320
    • Tao, N.1    Wagner, S.J.2    Lublin, D.M.3
  • 59
    • 0033592748 scopus 로고    scopus 로고
    • The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens
    • Underhill DM, Ozinsky A, Hajjar AM, et al. The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens. Nature. 1999;401(6755):811-815.
    • (1999) Nature , vol.401 , Issue.6755 , pp. 811-815
    • Underhill, D.M.1    Ozinsky, A.2    Hajjar, A.M.3
  • 60
    • 33644984194 scopus 로고    scopus 로고
    • Localization of TLR2 and MyD88 to Chlamydia trachomatis inclusions. Evidence for signaling by intracellular TLR2 during infection with an obligate intracellular pathogen
    • O'Connell CM, Ionova IA, Quayle AJ, Visintin A, Ingalls RR. Localization of TLR2 and MyD88 to Chlamydia trachomatis inclusions. Evidence for signaling by intracellular TLR2 during infection with an obligate intracellular pathogen. J Biol Chem. 2006;281(3):1652-1659.
    • (2006) J Biol Chem , vol.281 , Issue.3 , pp. 1652-1659
    • O'Connell, C.M.1    Ionova, I.A.2    Quayle, A.J.3    Visintin, A.4    Ingalls, R.R.5
  • 61
    • 79952750092 scopus 로고    scopus 로고
    • Phagosomal signaling by Borrelia burgdorferi in human monocytes involves Toll-like receptor (TLR) 2 and TLR8 cooperativity and TLR8-mediated induction of IFN-beta
    • Cervantes JL, Dunham-Ems SM, La Vake CJ, et al. Phagosomal signaling by Borrelia burgdorferi in human monocytes involves Toll-like receptor (TLR) 2 and TLR8 cooperativity and TLR8-mediated induction of IFN-beta. Proc Natl Acad Sci USA. 2011;108(9):3683-3688.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.9 , pp. 3683-3688
    • Cervantes, J.L.1    Dunham-Ems, S.M.2    La Vake, C.J.3
  • 62
    • 70350441863 scopus 로고    scopus 로고
    • Toll-like receptor 2 on inflammatory monocytes induces type I interferon in response to viral but not bacterial ligands
    • Barbalat R, Lau L, Locksley RM, Barton GM. Toll-like receptor 2 on inflammatory monocytes induces type I interferon in response to viral but not bacterial ligands. Nat Immunol. 2009;10(11):1200-1207.
    • (2009) Nat Immunol , vol.10 , Issue.11 , pp. 1200-1207
    • Barbalat, R.1    Lau, L.2    Locksley, R.M.3    Barton, G.M.4
  • 63
    • 34250837518 scopus 로고    scopus 로고
    • A novel role for HMGB1 in TLR9-mediated inflammatory responses to CpG-DNA
    • Ivanov S, Dragoi AM, Wang X, et al. A novel role for HMGB1 in TLR9-mediated inflammatory responses to CpG-DNA. Blood. 2007;110(6):1970-1981.
    • (2007) Blood , vol.110 , Issue.6 , pp. 1970-1981
    • Ivanov, S.1    Dragoi, A.M.2    Wang, X.3
  • 64
    • 34948862264 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide
    • Lande R, Gregorio J, Facchinetti V, et al. Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide. Nature. 2007;449(7162):564-569.
    • (2007) Nature , vol.449 , Issue.7162 , pp. 564-569
    • Lande, R.1    Gregorio, J.2    Facchinetti, V.3
  • 65
    • 84862804952 scopus 로고    scopus 로고
    • Accessory molecules for Toll-like receptors and their function
    • Lee CC, Avalos AM, Ploegh HL. Accessory molecules for Toll-like receptors and their function. Nat Rev Immunol. 2012;12(3):168-179.
    • (2012) Nat Rev Immunol , vol.12 , Issue.3 , pp. 168-179
    • Lee, C.C.1    Avalos, A.M.2    Ploegh, H.L.3
  • 66
    • 0027241980 scopus 로고
    • Purification of an autocrine growth factor homologous with mouse epithelin precursor from a highly tumorigenic cell line
    • Zhou J, Gao G, Crabb JW, Serrero G. Purification of an autocrine growth factor homologous with mouse epithelin precursor from a highly tumorigenic cell line. J Biol Chem. 1993;268(15):10863-10869.
    • (1993) J Biol Chem , vol.268 , Issue.15 , pp. 10863-10869
    • Zhou, J.1    Gao, G.2    Crabb, J.W.3    Serrero, G.4
  • 67
    • 79954570242 scopus 로고    scopus 로고
    • Granulin is a soluble cofactor for Toll-like receptor 9 signaling
    • Park B, Buti L, Lee S, et al. Granulin is a soluble cofactor for Toll-like receptor 9 signaling. Immunity. 2011;34(4):505-513.
    • (2011) Immunity , vol.34 , Issue.4 , pp. 505-513
    • Park, B.1    Buti, L.2    Lee, S.3
  • 68
    • 17144376810 scopus 로고    scopus 로고
    • High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal
    • Lotze MT, Tracey KJ. High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal. Nat Rev Immunol. 2005;5(4):331-342.
    • (2005) Nat Rev Immunol , vol.5 , Issue.4 , pp. 331-342
    • Lotze, M.T.1    Tracey, K.J.2
  • 69
    • 34247236200 scopus 로고    scopus 로고
    • Toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE
    • Tian J, Avalos AM, Mao SY, et al. Toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE. Nat Immunol. 2007;8(5):487-496.
    • (2007) Nat Immunol , vol.8 , Issue.5 , pp. 487-496
    • Tian, J.1    Avalos, A.M.2    Mao, S.Y.3
  • 70
    • 0031574103 scopus 로고    scopus 로고
    • The cathelicidin family of antimicrobial peptide precursors: a component of the oxygen-independent defense mechanisms of neutrophils
    • Zanetti M, Gennaro R, Romeo D. The cathelicidin family of antimicrobial peptide precursors: a component of the oxygen-independent defense mechanisms of neutrophils. Ann N Y Acad Sci. 1997;832:147-162.
    • (1997) Ann N Y Acad Sci , vol.832 , pp. 147-162
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 71
    • 77949315485 scopus 로고    scopus 로고
    • LL-37 promotes rapid sensing of CpG oligodeoxynucleotides by B lymphocytes and plasmacytoid dendritic cells
    • Hurtado P, Peh CA. LL-37 promotes rapid sensing of CpG oligodeoxynucleotides by B lymphocytes and plasmacytoid dendritic cells. J Immunol. 2010;184(3):1425-1435.
    • (2010) J Immunol , vol.184 , Issue.3 , pp. 1425-1435
    • Hurtado, P.1    Peh, C.A.2
  • 72
    • 48549088455 scopus 로고    scopus 로고
    • Antimicrobial peptides and self-DNA in autoimmune skin inflammation
    • Gilliet M, Lande R. Antimicrobial peptides and self-DNA in autoimmune skin inflammation. Curr Opin Immunol. 2008;20(4):401-407.
    • (2008) Curr Opin Immunol , vol.20 , Issue.4 , pp. 401-407
    • Gilliet, M.1    Lande, R.2
  • 73
    • 85047693371 scopus 로고    scopus 로고
    • Human lupus autoantibody-DNA complexes activate DCs through cooperation of CD32 and TLR9
    • Means TK, Latz E, Hayashi F, Murali MR, Golenbock DT, Luster AD. Human lupus autoantibody-DNA complexes activate DCs through cooperation of CD32 and TLR9. J Clin Invest. 2005;115(2):407-417.
    • (2005) J Clin Invest , vol.115 , Issue.2 , pp. 407-417
    • Means, T.K.1    Latz, E.2    Hayashi, F.3    Murali, M.R.4    Golenbock, D.T.5    Luster, A.D.6
  • 74
    • 5444274514 scopus 로고    scopus 로고
    • Interferon-alpha induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6
    • Kawai T, Sato S, Ishii KJ, et al. Interferon-alpha induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6. Nat Immunol. 2004;5(10):1061-1068.
    • (2004) Nat Immunol , vol.5 , Issue.10 , pp. 1061-1068
    • Kawai, T.1    Sato, S.2    Ishii, K.J.3
  • 75
    • 33645841633 scopus 로고    scopus 로고
    • IkappaB kinase-alpha is critical for interferon-alpha production induced by Toll-like receptors 7 and 9
    • Hoshino K, Sugiyama T, Matsumoto M, et al. IkappaB kinase-alpha is critical for interferon-alpha production induced by Toll-like receptors 7 and 9. Nature. 2006;440(7086):949-953.
    • (2006) Nature , vol.440 , Issue.7086 , pp. 949-953
    • Hoshino, K.1    Sugiyama, T.2    Matsumoto, M.3
  • 76
    • 17844380477 scopus 로고    scopus 로고
    • Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction
    • Honda K, Ohba Y, Yanai H, et al. Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction. Nature. 2005;434(7036):1035-1040.
    • (2005) Nature , vol.434 , Issue.7036 , pp. 1035-1040
    • Honda, K.1    Ohba, Y.2    Yanai, H.3
  • 77
    • 84894203179 scopus 로고    scopus 로고
    • A promiscuous lipid-binding protein diversifies the subcellular sites of toll-like receptor signal transduction
    • Bonham KS, Orzalli MH, Hayashi K, et al. A promiscuous lipid-binding protein diversifies the subcellular sites of toll-like receptor signal transduction. Cell. 2014;156(4):705-716.
    • (2014) Cell , vol.156 , Issue.4 , pp. 705-716
    • Bonham, K.S.1    Orzalli, M.H.2    Hayashi, K.3
  • 78
    • 77956689533 scopus 로고    scopus 로고
    • Bifurcation of Toll-like receptor 9 signaling by adaptor protein 3
    • Sasai M, Linehan MM, Iwasaki A. Bifurcation of Toll-like receptor 9 signaling by adaptor protein 3. Science. 2010;329(5998):1530-1534.
    • (2010) Science , vol.329 , Issue.5998 , pp. 1530-1534
    • Sasai, M.1    Linehan, M.M.2    Iwasaki, A.3
  • 79
    • 78649877815 scopus 로고    scopus 로고
    • Slc15a4, AP-3, and Hermansky-Pudlak syndrome proteins are required for Toll-like receptor signaling in plasmacytoid dendritic cells
    • Blasius AL, Arnold CN, Georgel P, et al. Slc15a4, AP-3, and Hermansky-Pudlak syndrome proteins are required for Toll-like receptor signaling in plasmacytoid dendritic cells. Proc Natl Acad Sci USA. 2010;107(46):19973-19978.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.46 , pp. 19973-19978
    • Blasius, A.L.1    Arnold, C.N.2    Georgel, P.3
  • 81
    • 84886797274 scopus 로고    scopus 로고
    • Autophagy in infection, inflammation and immunity
    • Deretic V, Saitoh T, Akira S. Autophagy in infection, inflammation and immunity. Nat Rev Immunol. 2013;13(10):722-737.
    • (2013) Nat Rev Immunol , vol.13 , Issue.10 , pp. 722-737
    • Deretic, V.1    Saitoh, T.2    Akira, S.3
  • 82
    • 84870861513 scopus 로고    scopus 로고
    • Noncanonical autophagy is required for type I interferon secretion in response to DNA-immune complexes
    • Henault J, Martinez J, Riggs JM, et al. Noncanonical autophagy is required for type I interferon secretion in response to DNA-immune complexes. Immunity. 2012;37(6):986-997.
    • (2012) Immunity , vol.37 , Issue.6 , pp. 986-997
    • Henault, J.1    Martinez, J.2    Riggs, J.M.3
  • 83
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • Levine B, Mizushima N, Virgin HW. Autophagy in immunity and inflammation. Nature. 2011;469(7330):323-335.
    • (2011) Nature , vol.469 , Issue.7330 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 84
    • 80054825045 scopus 로고    scopus 로고
    • Microtubule-associated protein 1 light chain 3 alpha (LC3)-associated phagocytosis is required for the efficient clearance of dead cells
    • Martinez J, Almendinger J, Oberst A, et al. Microtubule-associated protein 1 light chain 3 alpha (LC3)-associated phagocytosis is required for the efficient clearance of dead cells. Proc Natl Acad Sci USA. 2011;108(42):17396-17401.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.42 , pp. 17396-17401
    • Martinez, J.1    Almendinger, J.2    Oberst, A.3
  • 85
    • 37549043217 scopus 로고    scopus 로고
    • Toll-like receptor signalling in macrophages links the autophagy pathway to phagocytosis
    • Sanjuan MA, Dillon CP, Tait SW, et al. Toll-like receptor signalling in macrophages links the autophagy pathway to phagocytosis. Nature. 2007;450(7173):1253-1257.
    • (2007) Nature , vol.450 , Issue.7173 , pp. 1253-1257
    • Sanjuan, M.A.1    Dillon, C.P.2    Tait, S.W.3
  • 86
    • 84934287492 scopus 로고    scopus 로고
    • Molecular characterization of LC3-associated phagocytosis reveals distinct roles for Rubicon, NOX2 and autophagy proteins
    • Martinez J, Malireddi RK, Lu Q, et al. Molecular characterization of LC3-associated phagocytosis reveals distinct roles for Rubicon, NOX2 and autophagy proteins. Nat Cell Biol. 2015;17(7):893-906.
    • (2015) Nat Cell Biol , vol.17 , Issue.7 , pp. 893-906
    • Martinez, J.1    Malireddi, R.K.2    Lu, Q.3
  • 87
    • 84971328560 scopus 로고    scopus 로고
    • Noncanonical autophagy inhibits the autoinflammatory, lupus-like response to dying cells
    • Martinez J, Cunha LD, Park S, et al. Noncanonical autophagy inhibits the autoinflammatory, lupus-like response to dying cells. Nature. 2016;533(7601):115-119.
    • (2016) Nature , vol.533 , Issue.7601 , pp. 115-119
    • Martinez, J.1    Cunha, L.D.2    Park, S.3
  • 88
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo G, De Camilli P. Phosphoinositides in cell regulation and membrane dynamics. Nature. 2006;443(7112):651-657.
    • (2006) Nature , vol.443 , Issue.7112 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 89
    • 39549116503 scopus 로고    scopus 로고
    • PI3K is critical for the nuclear translocation of IRF-7 and type I IFN production by human plasmacytoid predendritic cells in response to TLR activation
    • Guiducci C, Ghirelli C, Marloie-Provost MA, et al. PI3K is critical for the nuclear translocation of IRF-7 and type I IFN production by human plasmacytoid predendritic cells in response to TLR activation. J Exp Med. 2008;205(2):315-322.
    • (2008) J Exp Med , vol.205 , Issue.2 , pp. 315-322
    • Guiducci, C.1    Ghirelli, C.2    Marloie-Provost, M.A.3
  • 90
    • 84940837203 scopus 로고    scopus 로고
    • Toll-like receptor 9 trafficking and signaling for type I interferons requires PIKfyve activity
    • Hayashi K, Sasai M, Iwasaki A. Toll-like receptor 9 trafficking and signaling for type I interferons requires PIKfyve activity. Int Immunol. 2015;27(9):435-445.
    • (2015) Int Immunol , vol.27 , Issue.9 , pp. 435-445
    • Hayashi, K.1    Sasai, M.2    Iwasaki, A.3
  • 91
    • 40049097361 scopus 로고    scopus 로고
    • Identification of plasmacytoid pre-dendritic cells by one-color flow cytometry for phenotype screening
    • Magyarics Z, Csillag A, Pazmandi K, Rajnavolgyi E, Bacsi A. Identification of plasmacytoid pre-dendritic cells by one-color flow cytometry for phenotype screening. Cytometry A. 2008;73(3):254-258.
    • (2008) Cytometry A , vol.73 , Issue.3 , pp. 254-258
    • Magyarics, Z.1    Csillag, A.2    Pazmandi, K.3    Rajnavolgyi, E.4    Bacsi, A.5
  • 92
    • 84880888092 scopus 로고    scopus 로고
    • PIKfyve, a class III PI kinase, is the target of the small molecular IL-12/IL-23 inhibitor apilimod and a player in Toll-like receptor signaling
    • Cai X, Xu Y, Cheung AK, et al. PIKfyve, a class III PI kinase, is the target of the small molecular IL-12/IL-23 inhibitor apilimod and a player in Toll-like receptor signaling. Chem Biol. 2013;20(7):912-921.
    • (2013) Chem Biol , vol.20 , Issue.7 , pp. 912-921
    • Cai, X.1    Xu, Y.2    Cheung, A.K.3
  • 93
    • 84897529123 scopus 로고    scopus 로고
    • PIKfyve, a class III lipid kinase, is required for TLR-induced type I IFN production via modulation of ATF3
    • Cai X, Xu Y, Kim YM, Loureiro J, Huang Q. PIKfyve, a class III lipid kinase, is required for TLR-induced type I IFN production via modulation of ATF3. J Immunol. 2014;192(7):3383-3389.
    • (2014) J Immunol , vol.192 , Issue.7 , pp. 3383-3389
    • Cai, X.1    Xu, Y.2    Kim, Y.M.3    Loureiro, J.4    Huang, Q.5
  • 94
    • 84922437081 scopus 로고    scopus 로고
    • Mucolipin 1 positively regulates TLR7 responses in dendritic cells by facilitating RNA transportation to lysosomes
    • Li X, Saitoh S, Shibata T, Tanimura N, Fukui R, Miyake K. Mucolipin 1 positively regulates TLR7 responses in dendritic cells by facilitating RNA transportation to lysosomes. Int Immunol. 2015;27(2):83-94.
    • (2015) Int Immunol , vol.27 , Issue.2 , pp. 83-94
    • Li, X.1    Saitoh, S.2    Shibata, T.3    Tanimura, N.4    Fukui, R.5    Miyake, K.6
  • 95
    • 84863392295 scopus 로고    scopus 로고
    • Cofactors required for TLR7- and TLR9-dependent innate immune responses
    • Chiang CY, Engel A, Opaluch AM, et al. Cofactors required for TLR7- and TLR9-dependent innate immune responses. Cell Host Microbe. 2012;11(3):306-318.
    • (2012) Cell Host Microbe , vol.11 , Issue.3 , pp. 306-318
    • Chiang, C.Y.1    Engel, A.2    Opaluch, A.M.3
  • 96
    • 84924794747 scopus 로고    scopus 로고
    • Emerging principles governing signal transduction by pattern-recognition receptors
    • Kagan JC, Barton GM. Emerging principles governing signal transduction by pattern-recognition receptors. Cold Spring Harb Perspect Biol. 2014;7(3):1-15.
    • (2014) Cold Spring Harb Perspect Biol , vol.7 , Issue.3 , pp. 1-15
    • Kagan, J.C.1    Barton, G.M.2
  • 97
    • 79953890803 scopus 로고    scopus 로고
    • The structural biology of Toll-like receptors
    • Botos I, Segal DM, Davies DR. The structural biology of Toll-like receptors. Structure. 2011;19(4):447-459.
    • (2011) Structure , vol.19 , Issue.4 , pp. 447-459
    • Botos, I.1    Segal, D.M.2    Davies, D.R.3
  • 98
    • 33646908228 scopus 로고    scopus 로고
    • Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling
    • Kagan JC, Medzhitov R. Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling. Cell. 2006;125(5):943-955.
    • (2006) Cell , vol.125 , Issue.5 , pp. 943-955
    • Kagan, J.C.1    Medzhitov, R.2
  • 99
    • 84922479840 scopus 로고    scopus 로고
    • SMOCs: supramolecular organizing centres that control innate immunity
    • Kagan JC, Magupalli VG, Wu H. SMOCs: supramolecular organizing centres that control innate immunity. Nat Rev Immunol. 2014;14(12):821-826.
    • (2014) Nat Rev Immunol , vol.14 , Issue.12 , pp. 821-826
    • Kagan, J.C.1    Magupalli, V.G.2    Wu, H.3
  • 100
    • 77953714711 scopus 로고    scopus 로고
    • Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling
    • Lin SC, Lo YC, Wu H. Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling. Nature. 2010;465(7300):885-890.
    • (2010) Nature , vol.465 , Issue.7300 , pp. 885-890
    • Lin, S.C.1    Lo, Y.C.2    Wu, H.3
  • 101
    • 84905050462 scopus 로고    scopus 로고
    • Assembly and localization of Toll-like receptor signalling complexes
    • Gay NJ, Symmons MF, Gangloff M, Bryant CE. Assembly and localization of Toll-like receptor signalling complexes. Nat Rev Immunol. 2014;14(8):546-558.
    • (2014) Nat Rev Immunol , vol.14 , Issue.8 , pp. 546-558
    • Gay, N.J.1    Symmons, M.F.2    Gangloff, M.3    Bryant, C.E.4
  • 102
    • 70349443224 scopus 로고    scopus 로고
    • Transcriptional control of the inflammatory response
    • Medzhitov R, Horng T. Transcriptional control of the inflammatory response. Nat Rev Immunol. 2009;9(10):692-703.
    • (2009) Nat Rev Immunol , vol.9 , Issue.10 , pp. 692-703
    • Medzhitov, R.1    Horng, T.2
  • 103
    • 79952100792 scopus 로고    scopus 로고
    • What the Myddosome structure tells us about the initiation of innate immunity
    • Gay NJ, Gangloff M, O'Neill LA. What the Myddosome structure tells us about the initiation of innate immunity. Trends Immunol. 2011;32(3):104-109.
    • (2011) Trends Immunol , vol.32 , Issue.3 , pp. 104-109
    • Gay, N.J.1    Gangloff, M.2    O'Neill, L.A.3
  • 104
    • 31344467156 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling 1 negatively regulates Toll-like receptor signaling by mediating Mal degradation
    • Mansell A, Smith R, Doyle SL, et al. Suppressor of cytokine signaling 1 negatively regulates Toll-like receptor signaling by mediating Mal degradation. Nat Immunol. 2006;7(2):148-155.
    • (2006) Nat Immunol , vol.7 , Issue.2 , pp. 148-155
    • Mansell, A.1    Smith, R.2    Doyle, S.L.3
  • 105
    • 84867713025 scopus 로고    scopus 로고
    • The p110delta isoform of the kinase PI(3)K controls the subcellular compartmentalization of TLR4 signaling and protects from endotoxic shock
    • Aksoy E, Taboubi S, Torres D, et al. The p110delta isoform of the kinase PI(3)K controls the subcellular compartmentalization of TLR4 signaling and protects from endotoxic shock. Nat Immunol. 2012;13(11):1045-1054.
    • (2012) Nat Immunol , vol.13 , Issue.11 , pp. 1045-1054
    • Aksoy, E.1    Taboubi, S.2    Torres, D.3
  • 106
    • 33744543517 scopus 로고    scopus 로고
    • MyD88 adapter-like (Mal) is phosphorylated by Bruton's tyrosine kinase during TLR2 and TLR4 signal transduction
    • Gray P, Dunne A, Brikos C, Jefferies CA, Doyle SL, O'Neill LA. MyD88 adapter-like (Mal) is phosphorylated by Bruton's tyrosine kinase during TLR2 and TLR4 signal transduction. J Biol Chem. 2006;281(15):10489-10495.
    • (2006) J Biol Chem , vol.281 , Issue.15 , pp. 10489-10495
    • Gray, P.1    Dunne, A.2    Brikos, C.3    Jefferies, C.A.4    Doyle, S.L.5    O'Neill, L.A.6
  • 107
    • 84933675709 scopus 로고    scopus 로고
    • A decoy peptide that disrupts TIRAP recruitment to TLRs is protective in a murine model of influenza
    • Piao W, Shirey KA, Ru LW, et al. A decoy peptide that disrupts TIRAP recruitment to TLRs is protective in a murine model of influenza. Cell Rep. 2015;11(12):1941-1952.
    • (2015) Cell Rep , vol.11 , Issue.12 , pp. 1941-1952
    • Piao, W.1    Shirey, K.A.2    Ru, L.W.3
  • 108
    • 33646567507 scopus 로고    scopus 로고
    • The myristoylation of TRIF-related adaptor molecule is essential for Toll-like receptor 4 signal transduction
    • Rowe DC, McGettrick AF, Latz E, et al. The myristoylation of TRIF-related adaptor molecule is essential for Toll-like receptor 4 signal transduction. Proc Natl Acad Sci USA. 2006;103(16):6299-6304.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.16 , pp. 6299-6304
    • Rowe, D.C.1    McGettrick, A.F.2    Latz, E.3
  • 109
    • 0038393016 scopus 로고    scopus 로고
    • IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway
    • Fitzgerald KA, McWhirter SM, Faia KL, et al. IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway. Nat Immunol. 2003;4(5):491-496.
    • (2003) Nat Immunol , vol.4 , Issue.5 , pp. 491-496
    • Fitzgerald, K.A.1    McWhirter, S.M.2    Faia, K.L.3
  • 110
    • 0038363463 scopus 로고    scopus 로고
    • Triggering the interferon antiviral response through an IKK-related pathway
    • Sharma S, tenOever BR, Grandvaux N, Zhou GP, Lin R, Hiscott J. Triggering the interferon antiviral response through an IKK-related pathway. Science. 2003;300(5622):1148-1151.
    • (2003) Science , vol.300 , Issue.5622 , pp. 1148-1151
    • Sharma, S.1    tenOever, B.R.2    Grandvaux, N.3    Zhou, G.P.4    Lin, R.5    Hiscott, J.6
  • 111
    • 74049136127 scopus 로고    scopus 로고
    • Different modes of ubiquitination of the adaptor TRAF3 selectively activate the expression of type I interferons and proinflammatory cytokines
    • Tseng PH, Matsuzawa A, Zhang W, Mino T, Vignali DA, Karin M. Different modes of ubiquitination of the adaptor TRAF3 selectively activate the expression of type I interferons and proinflammatory cytokines. Nat Immunol. 2010;11(1):70-75.
    • (2010) Nat Immunol , vol.11 , Issue.1 , pp. 70-75
    • Tseng, P.H.1    Matsuzawa, A.2    Zhang, W.3    Mino, T.4    Vignali, D.A.5    Karin, M.6
  • 112
    • 77956329223 scopus 로고    scopus 로고
    • Murine toll-like receptor 2 activation induces type I interferon responses from endolysosomal compartments
    • Dietrich N, Lienenklaus S, Weiss S, Gekara NO. Murine toll-like receptor 2 activation induces type I interferon responses from endolysosomal compartments. PLoS One. 2010;5(4):e10250.
    • (2010) PLoS One , vol.5 , Issue.4
    • Dietrich, N.1    Lienenklaus, S.2    Weiss, S.3    Gekara, N.O.4
  • 113
    • 84873054924 scopus 로고    scopus 로고
    • TRIF mediates Toll-like receptor 2-dependent inflammatory responses to Borrelia burgdorferi
    • Petnicki-Ocwieja T, Chung E, Acosta DI, et al. TRIF mediates Toll-like receptor 2-dependent inflammatory responses to Borrelia burgdorferi. Infect Immun. 2013;81(2):402-410.
    • (2013) Infect Immun , vol.81 , Issue.2 , pp. 402-410
    • Petnicki-Ocwieja, T.1    Chung, E.2    Acosta, D.I.3
  • 114
    • 84916917573 scopus 로고    scopus 로고
    • TRAM is required for TLR2 endosomal signaling to type I IFN induction
    • Stack J, Doyle SL, Connolly DJ, et al. TRAM is required for TLR2 endosomal signaling to type I IFN induction. J Immunol. 2014;193(12):6090-6102.
    • (2014) J Immunol , vol.193 , Issue.12 , pp. 6090-6102
    • Stack, J.1    Doyle, S.L.2    Connolly, D.J.3
  • 115
    • 84922311613 scopus 로고    scopus 로고
    • A role for the adaptor proteins TRAM and TRIF in toll-like receptor 2 signaling
    • Nilsen NJ, Vladimer GI, Stenvik J, et al. A role for the adaptor proteins TRAM and TRIF in toll-like receptor 2 signaling. J Biol Chem. 2015;290(6):3209-3222.
    • (2015) J Biol Chem , vol.290 , Issue.6 , pp. 3209-3222
    • Nilsen, N.J.1    Vladimer, G.I.2    Stenvik, J.3
  • 116
    • 84945156923 scopus 로고    scopus 로고
    • Adaptor protein-3-mediated trafficking of TLR2 ligands controls specificity of inflammatory responses but not adaptor complex assembly
    • Petnicki-Ocwieja T, Kern A, Killpack TL, Bunnell SC, Hu LT. Adaptor protein-3-mediated trafficking of TLR2 ligands controls specificity of inflammatory responses but not adaptor complex assembly. J Immunol. 2015;195(9):4331-4340.
    • (2015) J Immunol , vol.195 , Issue.9 , pp. 4331-4340
    • Petnicki-Ocwieja, T.1    Kern, A.2    Killpack, T.L.3    Bunnell, S.C.4    Hu, L.T.5


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