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Volumn 6, Issue , 2016, Pages

The N-terminal loop of IRAK-4 death domain regulates ordered assembly of the Myddosome signalling scaffold

Author keywords

[No Author keywords available]

Indexed keywords

INTERLEUKIN 1 RECEPTOR ASSOCIATED KINASE; IRAK4 PROTEIN, HUMAN; MULTIPROTEIN COMPLEX; MYD88 PROTEIN, HUMAN; MYELOID DIFFERENTIATION FACTOR 88;

EID: 84996523762     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep37267     Document Type: Article
Times cited : (19)

References (39)
  • 1
    • 84905050462 scopus 로고    scopus 로고
    • Assembly and localization of Toll-like receptor signalling complexes
    • Gay, N. J., Symmons, M. F., Gangloff, M. & Bryant, C. E. Assembly and localization of Toll-like receptor signalling complexes. Nature Rev. Immunol. 14, 546-558 (2014).
    • (2014) Nature Rev. Immunol. , vol.14 , pp. 546-558
    • Gay, N.J.1    Symmons, M.F.2    Gangloff, M.3    Bryant, C.E.4
  • 2
    • 79959447465 scopus 로고    scopus 로고
    • Structural biology of the Toll-like receptor family
    • Kang, J. Y. & Lee, J. O. Structural biology of the Toll-like receptor family. Annu. Rev. Biochem. 80, 917-941 (2011).
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 917-941
    • Kang, J.Y.1    Lee, J.O.2
  • 4
    • 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. 284, 25404-25411 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 25404-25411
    • Motshwene, P.G.1
  • 5
    • 77953714711 scopus 로고    scopus 로고
    • Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling
    • Lin, S. C., Lo, Y. C. & Wu, H. Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling. Nature 465, 885-890 (2010).
    • (2010) Nature , vol.465 , pp. 885-890
    • Lin, S.C.1    Lo, Y.C.2    Wu, H.3
  • 6
    • 84862777437 scopus 로고    scopus 로고
    • Helical assembly in the death domain (DD) superfamily
    • Ferrao, R. & Wu, H. Helical assembly in the death domain (DD) superfamily. Curr. Opin. Struct. Biol. 22, 241-247 (2012).
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 241-247
    • Ferrao, R.1    Wu, H.2
  • 7
    • 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. 26, 475-481 (2001).
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 475-481
    • Weber, C.H.1    Vincenz, C.2
  • 8
    • 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 128, 533-546 (2007).
    • (2007) Cell , vol.128 , pp. 533-546
    • Park, H.H.1
  • 9
    • 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 321, 691-696 (2008).
    • (2008) Science , vol.321 , pp. 691-696
    • Von Bernuth, H.1
  • 10
    • 0037471003 scopus 로고    scopus 로고
    • Pyogenic bacterial infections in humans with IRAK-4 deficiency
    • Picard, C. et al. Pyogenic bacterial infections in humans with IRAK-4 deficiency. Science 299, 2076-2079 (2003).
    • (2003) Science , vol.299 , pp. 2076-2079
    • Picard, C.1
  • 11
    • 39249084649 scopus 로고    scopus 로고
    • TLR9 activation induces normal neutrophil responses in a child with IRAK-4 deficiency: Involvement of the direct PI3K pathway
    • Hoarau, C. et al. TLR9 activation induces normal neutrophil responses in a child with IRAK-4 deficiency: involvement of the direct PI3K pathway. J. Immunol. 179, 4754-4765 (2007).
    • (2007) J. Immunol. , vol.179 , pp. 4754-4765
    • Hoarau, C.1
  • 12
    • 84919473543 scopus 로고    scopus 로고
    • Activation of lymphoma-associated MyD88 mutations via allostery-induced TIR-domain oligomerization
    • Avbelj, M. et al. Activation of lymphoma-associated MyD88 mutations via allostery-induced TIR-domain oligomerization. Blood 124, 3896-3904 (2014).
    • (2014) Blood , vol.124 , pp. 3896-3904
    • Avbelj, M.1
  • 13
    • 79551686422 scopus 로고    scopus 로고
    • Oncogenically active MYD88 mutations in human lymphoma
    • Ngo, V. N. et al. Oncogenically active MYD88 mutations in human lymphoma. Nature 470, 115-119 (2011).
    • (2011) Nature , vol.470 , pp. 115-119
    • Ngo, V.N.1
  • 14
    • 84907975948 scopus 로고    scopus 로고
    • IRAK4 Dimerization and trans-Autophosphorylation Are Induced by Myddosome Assembly
    • Ferrao, R. et al. IRAK4 Dimerization and trans-Autophosphorylation Are Induced by Myddosome Assembly. Mol. Cell 55, 891-903 (2014).
    • (2014) Mol. Cell , vol.55 , pp. 891-903
    • Ferrao, R.1
  • 15
    • 34249095729 scopus 로고    scopus 로고
    • Essential role of IRAK-4 protein and its kinase activity in Toll-like receptor-mediated immune responses but not in TCR signaling
    • Kawagoe, T. et al. Essential role of IRAK-4 protein and its kinase activity in Toll-like receptor-mediated immune responses but not in TCR signaling. J. Exp. Med. 204, 1013-1024 (2007).
    • (2007) J. Exp. Med. , vol.204 , pp. 1013-1024
    • Kawagoe, T.1
  • 16
    • 34249078495 scopus 로고    scopus 로고
    • A critical role for IRAK4 kinase activity in Toll-like receptor-mediated innate immunity
    • Kim, T. W. et al. A critical role for IRAK4 kinase activity in Toll-like receptor-mediated innate immunity. J. Exp. Med. 204, 1025-1036 (2007).
    • (2007) J. Exp. Med. , vol.204 , pp. 1025-1036
    • Kim, T.W.1
  • 17
    • 33845316120 scopus 로고    scopus 로고
    • Regulation of IRAK-4 kinase activity via autophosphorylation within its activation loop
    • Cheng, H. et al. Regulation of IRAK-4 kinase activity via autophosphorylation within its activation loop. Biochem. Biophys. Res. Commun. 352, 609-616 (2007).
    • (2007) Biochem. Biophys. Res. Commun. , vol.352 , pp. 609-616
    • Cheng, H.1
  • 18
    • 84857598530 scopus 로고    scopus 로고
    • The extended cleavage specificity of human thrombin
    • Gallwitz, M., Enoksson, M., Thorpe, M. & Hellman, L. The extended cleavage specificity of human thrombin. PLoS One 7, e31756 (2012).
    • (2012) PLoS One , vol.7
    • Gallwitz, M.1    Enoksson, M.2    Thorpe, M.3    Hellman, L.4
  • 19
    • 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. 286, 1341-1353 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 1341-1353
    • George, J.1
  • 20
    • 25444503240 scopus 로고    scopus 로고
    • Cutting edge: Molecular structure of the IL-1R-associated kinase-4 death domain and its implications for TLR signaling
    • Lasker, M. V., Gajjar, M. M. & Nair, S. K. Cutting edge: molecular structure of the IL-1R-associated kinase-4 death domain and its implications for TLR signaling. J. Immunol. 175, 4175-4179 (2005).
    • (2005) J. Immunol. , vol.175 , pp. 4175-4179
    • Lasker, M.V.1    Gajjar, M.M.2    Nair, S.K.3
  • 21
    • 0037065734 scopus 로고    scopus 로고
    • Effect of phosphorylation on alpha-helix stability as a function of position
    • Andrew, C. D., Warwicker, J., Jones, G. R. & Doig, A. J. Effect of phosphorylation on alpha-helix stability as a function of position. Biochemistry. 41, 1897-1905 (2002).
    • (2002) Biochemistry. , vol.41 , pp. 1897-1905
    • Andrew, C.D.1    Warwicker, J.2    Jones, G.R.3    Doig, A.J.4
  • 22
    • 84911894047 scopus 로고    scopus 로고
    • Molecular determinants of caspase-9 activation by the Apaf-1 apoptosome
    • Hu, Q. et al. Molecular determinants of caspase-9 activation by the Apaf-1 apoptosome. Proc. Natl. Acad. Sci. USA 111, 16254-16261 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 16254-16261
    • Hu, Q.1
  • 23
    • 33846630988 scopus 로고    scopus 로고
    • Strengths of hydrogen bonds involving phosphorylated amino acid side chains
    • Mandell, D. J. et al. Strengths of hydrogen bonds involving phosphorylated amino acid side chains. J. Am. Chem. Soc. 129, 820-827 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 820-827
    • Mandell, D.J.1
  • 24
    • 84922479840 scopus 로고    scopus 로고
    • SMOCs: Supramolecular organizing centres that control innate immunity
    • Kagan, J. C., Magupalli, V. G. & Wu, H. SMOCs: supramolecular organizing centres that control innate immunity. Nature Rev. Immunol. 14, 821-826 (2014).
    • (2014) Nature Rev. Immunol. , vol.14 , pp. 821-826
    • Kagan, J.C.1    Magupalli, V.G.2    Wu, H.3
  • 25
    • 70350356853 scopus 로고    scopus 로고
    • Activating immunity: Lessons from the TLRs and NLRs
    • Monie, T. P., Bryant, C. E. & Gay, N. J. Activating immunity: lessons from the TLRs and NLRs. Trends Biochem. Sci. 34, 553-561 (2009).
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 553-561
    • Monie, T.P.1    Bryant, C.E.2    Gay, N.J.3
  • 26
    • 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. Nature Struct. Mol. Biol. 17, 1324-1329 (2010).
    • (2010) Nature Struct. Mol. Biol. , vol.17 , pp. 1324-1329
    • Wang, L.1
  • 27
    • 84889571746 scopus 로고    scopus 로고
    • Functional assessment of the mutational effects of human IRAK4 and MyD88 genes
    • Yamamoto, T. et al. Functional assessment of the mutational effects of human IRAK4 and MyD88 genes. Mol. Immunol. 58, 66-76 (2014).
    • (2014) Mol. Immunol. , vol.58 , pp. 66-76
    • Yamamoto, T.1
  • 28
    • 0026033985 scopus 로고
    • Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP
    • Barford, D., Hu, S. H. & Johnson, L. N. Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP. J. Mol. Biol. 218, 233-260 (1991).
    • (1991) J. Mol. Biol. , vol.218 , pp. 233-260
    • Barford, D.1    Hu, S.H.2    Johnson, L.N.3
  • 29
    • 84875219876 scopus 로고    scopus 로고
    • IRAK-M mediates Toll-like receptor/IL-1R-induced NFkappaB activation and cytokine production
    • Zhou, H. et al. IRAK-M mediates Toll-like receptor/IL-1R-induced NFkappaB activation and cytokine production. EMBO J 32, 583-596 (2013).
    • (2013) EMBO J , vol.32 , pp. 583-596
    • Zhou, H.1
  • 30
    • 77952370155 scopus 로고    scopus 로고
    • Tube Is an IRAK-4 homolog in a Toll pathway adapted for development and immunity
    • Towb, P., Sun, H. & Wasserman, S. A. Tube Is an IRAK-4 homolog in a Toll pathway adapted for development and immunity. J Innate Immun. 1, 309-321 (2009).
    • (2009) J Innate Immun. , vol.1 , pp. 309-321
    • Towb, P.1    Sun, H.2    Wasserman, S.A.3
  • 31
    • 57749089751 scopus 로고    scopus 로고
    • Assembly of oligomeric death domain complexes during toll receptor signaling
    • Moncrieffe, M. C., Grossmann, J. G. & Gay, N. J. Assembly of Oligomeric Death Domain Complexes during Toll Receptor Signaling. J. Biol. Chem. 283, 33447-33454 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 33447-33454
    • Moncrieffe, M.C.1    Grossmann, J.G.2    Gay, N.J.3
  • 32
    • 0842307067 scopus 로고    scopus 로고
    • Regulated assembly of the Toll signaling complex drives Drosophila dorsoventral patterning
    • Sun, H., Towb, P., Chiem, D. N., Foster, B. A. & Wasserman, S. A. Regulated assembly of the Toll signaling complex drives Drosophila dorsoventral patterning. EMBO J. 23, 100-110 (2004).
    • (2004) EMBO J. , vol.23 , pp. 100-110
    • Sun, H.1    Towb, P.2    Chiem, D.N.3    Foster, B.A.4    Wasserman, S.A.5
  • 33
    • 0033601077 scopus 로고    scopus 로고
    • Three-dimensional structure of a complex between the death domains of Pelle and Tube
    • Xiao, T., Towb, P., Wasserman, S. A. & Sprang, S. R. Three-dimensional structure of a complex between the death domains of Pelle and Tube. Cell 99, 545-555 (1999).
    • (1999) Cell , vol.99 , pp. 545-555
    • Xiao, T.1    Towb, P.2    Wasserman, S.A.3    Sprang, S.R.4
  • 34
    • 0030815382 scopus 로고    scopus 로고
    • An activity-dependent network of interactions links the Rel protein Dorsal with its cytoplasmic regulators
    • Edwards, D. N., Towb, P. & Wasserman, S. A. An activity-dependent network of interactions links the Rel protein Dorsal with its cytoplasmic regulators. Development 124, 3855-3864 (1997).
    • (1997) Development , vol.124 , pp. 3855-3864
    • Edwards, D.N.1    Towb, P.2    Wasserman, S.A.3
  • 35
    • 84884511455 scopus 로고    scopus 로고
    • The IRAK homolog Pelle is the functional counterpart of IkappaB kinase in the Drosophila Toll pathway
    • Daigneault, J., Klemetsaune, L. & Wasserman, S. A. The IRAK homolog Pelle is the functional counterpart of IkappaB kinase in the Drosophila Toll pathway. PLoS One 8, e75150 (2013).
    • (2013) PLoS One , vol.8
    • Daigneault, J.1    Klemetsaune, L.2    Wasserman, S.A.3
  • 36
    • 0037117543 scopus 로고    scopus 로고
    • IRAK-4: A novel member of the IRAK family with the properties of an IRAKkinase
    • Li, S. Y., Strelow, A., Fontana, E. J. & Wesche, H. IRAK-4: A novel member of the IRAK family with the properties of an IRAKkinase. Proc. Natl. Acad. Sci. USA 99, 5567-5572 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5567-5572
    • Li, S.Y.1    Strelow, A.2    Fontana, E.J.3    Wesche, H.4
  • 37
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. & Mann, M. Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels. Anal. Chem. 68, 850-858 (1996).
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 38
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm, M. et al. Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 379, 466-469 (1996).
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1


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