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Volumn 32, Issue 3, 2011, Pages 104-109

What the Myddosome structure tells us about the initiation of innate immunity

Author keywords

[No Author keywords available]

Indexed keywords

INTERLEUKIN 1 RECEPTOR; INTERLEUKIN 1 RECEPTOR ASSOCIATED KINASE 1; INTERLEUKIN 1 RECEPTOR ASSOCIATED KINASE 2; INTERLEUKIN 1 RECEPTOR ASSOCIATED KINASE 4; MULTIPROTEIN COMPLEX; MYELOID DIFFERENTIATION FACTOR 88; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR ADAPTOR MOLECULE 1;

EID: 79952100792     PISSN: 14714906     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.it.2010.12.005     Document Type: Review
Times cited : (155)

References (35)
  • 1
    • 34247566510 scopus 로고    scopus 로고
    • The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling
    • O'Neill L.A., Bowie A.G. The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling. Nat. Rev. Immunol. 2007, 7:353-364.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 353-364
    • O'Neill, L.A.1    Bowie, A.G.2
  • 2
    • 70350356853 scopus 로고    scopus 로고
    • Activating immunity: lessons from the TLRs and NLRs
    • Monie T.P., et al. Activating immunity: lessons from the TLRs and NLRs. Trends Biochem. Sci. 2009, 34:553-561.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 553-561
    • Monie, T.P.1
  • 3
    • 77950542752 scopus 로고    scopus 로고
    • Targeting Toll-like receptors: emerging therapeutics? Nat
    • Hennessy E.J., et al. Targeting Toll-like receptors: emerging therapeutics? Nat. Rev. Drug. Discov. 2010, 9:293-307.
    • (2010) Rev. Drug. Discov. , vol.9 , pp. 293-307
    • Hennessy, E.J.1
  • 4
    • 35649022764 scopus 로고    scopus 로고
    • Kinase-active interleukin-1 receptor-associated kinases promote polyubiquitination and degradation of the Pellino family: direct evidence for PELLINO proteins being ubiquitin-protein isopeptide ligases
    • Butler M.P., et al. Kinase-active interleukin-1 receptor-associated kinases promote polyubiquitination and degradation of the Pellino family: direct evidence for PELLINO proteins being ubiquitin-protein isopeptide ligases. J. Biol. Chem. 2007, 282:29729-29737.
    • (2007) J. Biol. Chem. , vol.282 , pp. 29729-29737
    • Butler, M.P.1
  • 5
    • 77953302679 scopus 로고    scopus 로고
    • IRAK1 and IRAK4 promote phosphorylation, ubiquitination, and degradation of MyD88 adaptor-like (Mal)
    • Dunne A., et al. IRAK1 and IRAK4 promote phosphorylation, ubiquitination, and degradation of MyD88 adaptor-like (Mal). J. Biol. Chem. 2010, 285:18276-18282.
    • (2010) J. Biol. Chem. , vol.285 , pp. 18276-18282
    • Dunne, A.1
  • 6
    • 36348932904 scopus 로고    scopus 로고
    • IRAK-2 participates in multiple toll-like receptor signaling pathways to NFkappaB via activation of TRAF6 ubiquitination
    • Keating S.E., et al. IRAK-2 participates in multiple toll-like receptor signaling pathways to NFkappaB via activation of TRAF6 ubiquitination. J. Biol. Chem. 2007, 282:33435-33443.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33435-33443
    • Keating, S.E.1
  • 7
    • 33744543517 scopus 로고    scopus 로고
    • MyD88 adapter-like (Mal) is phosphorylated by Bruton's tyrosine kinase during TLR2 and TLR4 signal transduction
    • Gray P., et al. MyD88 adapter-like (Mal) is phosphorylated by Bruton's tyrosine kinase during TLR2 and TLR4 signal transduction. J. Biol. Chem. 2006, 281:10489-10495.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10489-10495
    • Gray, P.1
  • 8
    • 31344467156 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling 1 negatively regulates Toll-like receptor signaling by mediating Mal degradation
    • Mansell A., et al. Suppressor of cytokine signaling 1 negatively regulates Toll-like receptor signaling by mediating Mal degradation. Nat. Immunol. 2006, 7:148-155.
    • (2006) Nat. Immunol. , vol.7 , pp. 148-155
    • Mansell, A.1
  • 9
    • 33745124663 scopus 로고    scopus 로고
    • Trif-related adapter molecule is phosphorylated by PKC{varepsilon} during Toll-like receptor 4 signaling
    • McGettrick A.F., et al. Trif-related adapter molecule is phosphorylated by PKC{varepsilon} during Toll-like receptor 4 signaling. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:9196-9201.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 9196-9201
    • McGettrick, A.F.1
  • 10
    • 33748871187 scopus 로고    scopus 로고
    • The human adaptor SARM negatively regulates adaptor protein TRIF-dependent Toll-like receptor signaling
    • Carty M., et al. The human adaptor SARM negatively regulates adaptor protein TRIF-dependent Toll-like receptor signaling. Nat. Immunol. 2006, 7:1074-1081.
    • (2006) Nat. Immunol. , vol.7 , pp. 1074-1081
    • Carty, M.1
  • 11
    • 34047098731 scopus 로고    scopus 로고
    • A Mal functional variant is associated with protection against invasive pneumococcal disease, bacteremia, malaria and tuberculosis
    • Khor C.C., et al. A Mal functional variant is associated with protection against invasive pneumococcal disease, bacteremia, malaria and tuberculosis. Nat. Genet. 2007, 39:523-528.
    • (2007) Nat. Genet. , vol.39 , pp. 523-528
    • Khor, C.C.1
  • 12
    • 77957846970 scopus 로고    scopus 로고
    • Association between single-nucleotide polymorphisms in Mal/TIRAP and interleukin-10 genes and susceptibility to invasive Haemophilus influenzae serotype b infection in immunized children
    • Ladhani S.N., et al. Association between single-nucleotide polymorphisms in Mal/TIRAP and interleukin-10 genes and susceptibility to invasive Haemophilus influenzae serotype b infection in immunized children. Clin. Infect. Dis. 2010, 51:761-767.
    • (2010) Clin. Infect. Dis. , vol.51 , pp. 761-767
    • Ladhani, S.N.1
  • 13
    • 67649880546 scopus 로고    scopus 로고
    • Functional and genetic evidence that the Mal/TIRAP allele variant 180L has been selected by providing protection against septic shock
    • Ferwerda B., et al. Functional and genetic evidence that the Mal/TIRAP allele variant 180L has been selected by providing protection against septic shock. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:10272-10277.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 10272-10277
    • Ferwerda, B.1
  • 14
    • 48749109290 scopus 로고    scopus 로고
    • Pyogenic bacterial infections in humans with MyD88 deficiency
    • von Bernuth H., et al. Pyogenic bacterial infections in humans with MyD88 deficiency. Science 2008, 321:691-696.
    • (2008) Science , vol.321 , pp. 691-696
    • von Bernuth, H.1
  • 15
    • 48749127416 scopus 로고    scopus 로고
    • Elucidation of the MD-2/TLR4 interface required for signaling by lipid IVa
    • Walsh C., et al. Elucidation of the MD-2/TLR4 interface required for signaling by lipid IVa. J. Immunol. 2008, 181:1245-1254.
    • (2008) J. Immunol. , vol.181 , pp. 1245-1254
    • Walsh, C.1
  • 16
    • 69949161905 scopus 로고    scopus 로고
    • An oligomeric signaling platform formed by the Toll-like receptor signal transducers MyD88 and IRAK-4
    • Motshwene P.G., et al. An oligomeric signaling platform formed by the Toll-like receptor signal transducers MyD88 and IRAK-4. J. Biol. Chem. 2009, 284:25404-25411.
    • (2009) J. Biol. Chem. , vol.284 , pp. 25404-25411
    • Motshwene, P.G.1
  • 17
    • 77953714711 scopus 로고    scopus 로고
    • Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling
    • Lin S.C., et al. Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling. Nature 2010, 465:885-890.
    • (2010) Nature , vol.465 , pp. 885-890
    • Lin, S.C.1
  • 18
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex
    • Park B.S., et al. The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature 2009, 458:1191-1195.
    • (2009) Nature , vol.458 , pp. 1191-1195
    • Park, B.S.1
  • 19
    • 34548608447 scopus 로고    scopus 로고
    • Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide
    • Jin M.S., et al. Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide. Cell 2007, 130:1071-1082.
    • (2007) Cell , vol.130 , pp. 1071-1082
    • Jin, M.S.1
  • 20
    • 42349090335 scopus 로고    scopus 로고
    • Structural basis of toll-like receptor 3 signaling with double-stranded RNA
    • Liu L., et al. Structural basis of toll-like receptor 3 signaling with double-stranded RNA. Science 2008, 320:379-381.
    • (2008) Science , vol.320 , pp. 379-381
    • Liu, L.1
  • 21
    • 33748090945 scopus 로고    scopus 로고
    • Toll-like receptors as molecular switches
    • Gay N.J., et al. Toll-like receptors as molecular switches. Nat. Rev. Immunol. 2006, 6:693-698.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 693-698
    • Gay, N.J.1
  • 22
    • 40749097627 scopus 로고    scopus 로고
    • A dimer of the Toll-like receptor 4 cytoplasmic domain provides a specific scaffold for the recruitment of signalling adaptor proteins
    • Nunez Miguel R., et al. A dimer of the Toll-like receptor 4 cytoplasmic domain provides a specific scaffold for the recruitment of signalling adaptor proteins. PLoS One 2007, 2:e788.
    • (2007) PLoS One , vol.2
    • Nunez Miguel, R.1
  • 23
    • 40949134086 scopus 로고    scopus 로고
    • TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-beta
    • Kagan J.C., et al. TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-beta. Nat. Immunol. 2008, 9:361-368.
    • (2008) Nat. Immunol. , vol.9 , pp. 361-368
    • Kagan, J.C.1
  • 24
    • 33646908228 scopus 로고    scopus 로고
    • Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling
    • Kagan J.C., Medzhitov R. Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling. Cell 2006, 125:943-955.
    • (2006) Cell , vol.125 , pp. 943-955
    • Kagan, J.C.1    Medzhitov, R.2
  • 25
    • 33646567507 scopus 로고    scopus 로고
    • The myristoylation of TRIF-related adaptor molecule is essential for Toll-like receptor 4 signal transduction
    • Rowe D.C., et al. The myristoylation of TRIF-related adaptor molecule is essential for Toll-like receptor 4 signal transduction. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:6299-6304.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 6299-6304
    • Rowe, D.C.1
  • 26
    • 34548459868 scopus 로고    scopus 로고
    • Structure and function of Toll receptors and their ligands
    • Gay N.J., Gangloff M. Structure and function of Toll receptors and their ligands. Annu. Rev. Biochem. 2007, 76:141-165.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 141-165
    • Gay, N.J.1    Gangloff, M.2
  • 27
    • 0035425256 scopus 로고    scopus 로고
    • The death domain superfamily: a tale of two interfaces?
    • Weber C.H., Vincenz C. The death domain superfamily: a tale of two interfaces?. Trends Biochem. Sci. 2001, 26:475-481.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 475-481
    • Weber, C.H.1    Vincenz, C.2
  • 28
    • 34247842740 scopus 로고    scopus 로고
    • The death domain superfamily in intracellular signaling of apoptosis and inflammation
    • Park H.H., et al. The death domain superfamily in intracellular signaling of apoptosis and inflammation. Annu. Rev. Immunol. 2007, 25:561-586.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 561-586
    • Park, H.H.1
  • 29
    • 33846702221 scopus 로고    scopus 로고
    • Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex
    • Park H.H., et al. Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex. Cell 2007, 128:533-546.
    • (2007) Cell , vol.128 , pp. 533-546
    • Park, H.H.1
  • 30
    • 78651399661 scopus 로고    scopus 로고
    • Two human MYD88 variants, S34Y and R98C, interfere with MYD88-IRAK4-myddosome assembly
    • George J., et al. Two human MYD88 variants, S34Y and R98C, interfere with MYD88-IRAK4-myddosome assembly. J. Biol. Chem. 2011, 286:1341-1353.
    • (2011) J. Biol. Chem. , vol.286 , pp. 1341-1353
    • George, J.1
  • 31
    • 57749089751 scopus 로고    scopus 로고
    • Assembly of oligomeric death domain complexes during Toll receptor signaling
    • Moncrieffe M.C., et al. Assembly of oligomeric death domain complexes during Toll receptor signaling. J. Biol. Chem. 2008, 283:33447-33454.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33447-33454
    • Moncrieffe, M.C.1
  • 32
    • 33748363077 scopus 로고    scopus 로고
    • Dynamically driven protein allostery
    • Popovych N., et al. Dynamically driven protein allostery. Nat. Struct. Mol. Biol. 2006, 13:831-838.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 831-838
    • Popovych, N.1
  • 33
    • 60549106191 scopus 로고    scopus 로고
    • The Fas-FADD death domain complex structure unravels signalling by receptor clustering
    • Scott F.L., et al. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. Nature 2009, 457:1019-1022.
    • (2009) Nature , vol.457 , pp. 1019-1022
    • Scott, F.L.1
  • 34
    • 78549236456 scopus 로고    scopus 로고
    • The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations
    • Wang L., et al. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nat. Struct. Mol. Biol. 2010, 17:1324-1329.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1324-1329
    • Wang, L.1
  • 35
    • 70349308508 scopus 로고    scopus 로고
    • Cell regulation: determined to signal discrete cooperation
    • Gibson T.J. Cell regulation: determined to signal discrete cooperation. Trends Biochem. Sci. 2009, 34:471-482.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 471-482
    • Gibson, T.J.1


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