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Volumn 15, Issue 6-7, 2013, Pages 516-523

Roles of NLRP10 in innate and adaptive immunity

Author keywords

ASC; Dendritic cells; Dermatitis; Inflammasome; Innate immunity; NLR; NOD1; Skin

Indexed keywords

ACTIN; CARRIER PROTEIN; INFLAMMASOME; NUCLEOTIDE BINDING DOMAIN LEUCINE RICH REPEAT CONTAINING PROTEIN 10; UNCLASSIFIED DRUG;

EID: 84879184506     PISSN: 12864579     EISSN: 1769714X     Source Type: Journal    
DOI: 10.1016/j.micinf.2013.03.008     Document Type: Short Survey
Times cited : (28)

References (76)
  • 1
    • 31344461659 scopus 로고    scopus 로고
    • Innate immune recognition of viral infection
    • Kawai T., Akira S. Innate immune recognition of viral infection. Nat. Immunol. 2006, 7:131-137.
    • (2006) Nat. Immunol. , vol.7 , pp. 131-137
    • Kawai, T.1    Akira, S.2
  • 2
    • 73549090166 scopus 로고    scopus 로고
    • Identification of host cytosolic sensors and bacterial factors regulating the type I interferon response to Legionella pneumophila
    • Monroe K.M., McWhirter S.M., Vance R.E. Identification of host cytosolic sensors and bacterial factors regulating the type I interferon response to Legionella pneumophila. PLoS Pathog. 2009, 5:e1000665.
    • (2009) PLoS Pathog. , vol.5
    • Monroe, K.M.1    McWhirter, S.M.2    Vance, R.E.3
  • 3
    • 0033966411 scopus 로고    scopus 로고
    • Toll signaling pathways in the innate immune response
    • Anderson K.V. Toll signaling pathways in the innate immune response. Curr. Opin. Immunol. 2000, 12:13-19.
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 13-19
    • Anderson, K.V.1
  • 4
    • 84865411904 scopus 로고    scopus 로고
    • C-type lectin receptors orchestrate antifungal immunity
    • Hardison S.E., Brown G.D. C-type lectin receptors orchestrate antifungal immunity. Nat. Immunol. 2012, 13:817-822.
    • (2012) Nat. Immunol. , vol.13 , pp. 817-822
    • Hardison, S.E.1    Brown, G.D.2
  • 5
    • 35348932070 scopus 로고    scopus 로고
    • Intracellular NOD-like receptors in host defense and disease
    • Kanneganti T.D., Lamkanfi M., Nunez G. Intracellular NOD-like receptors in host defense and disease. Immunity 2007, 27:549-559.
    • (2007) Immunity , vol.27 , pp. 549-559
    • Kanneganti, T.D.1    Lamkanfi, M.2    Nunez, G.3
  • 7
    • 33746028777 scopus 로고    scopus 로고
    • Intracellular pattern recognition receptors in the host response
    • Meylan E., Tschopp J., Karin M. Intracellular pattern recognition receptors in the host response. Nature 2006, 442:39-44.
    • (2006) Nature , vol.442 , pp. 39-44
    • Meylan, E.1    Tschopp, J.2    Karin, M.3
  • 8
    • 77950476766 scopus 로고    scopus 로고
    • Sensing and signaling in antiviral innate immunity
    • O'Neill L.A., Bowie A.G. Sensing and signaling in antiviral innate immunity. Curr. Biol. 2010, 20:R328-R333.
    • (2010) Curr. Biol. , vol.20
    • O'Neill, L.A.1    Bowie, A.G.2
  • 9
    • 39149116674 scopus 로고    scopus 로고
    • NLR, the nucleotide-binding domain leucine-rich repeat containing gene family
    • Ye Z., Ting J.P. NLR, the nucleotide-binding domain leucine-rich repeat containing gene family. Curr. Opin. Immunol. 2008, 20:3-9.
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 3-9
    • Ye, Z.1    Ting, J.P.2
  • 10
    • 0037833742 scopus 로고    scopus 로고
    • Caspase-activation pathways in apoptosis and immunity
    • Creagh E.M., Conroy H., Martin S.J. Caspase-activation pathways in apoptosis and immunity. Immunol. Rev. 2003, 193:10-21.
    • (2003) Immunol. Rev. , vol.193 , pp. 10-21
    • Creagh, E.M.1    Conroy, H.2    Martin, S.J.3
  • 11
    • 33747191203 scopus 로고    scopus 로고
    • The inflammasome: first line of the immune response to cell stress
    • Ogura Y., Sutterwala F.S., Flavell R.A. The inflammasome: first line of the immune response to cell stress. Cell 2006, 126:659-662.
    • (2006) Cell , vol.126 , pp. 659-662
    • Ogura, Y.1    Sutterwala, F.S.2    Flavell, R.A.3
  • 12
    • 77649179433 scopus 로고    scopus 로고
    • NLRP3 inflammasome activation: the convergence of multiple signalling pathways on ROS production?
    • Tschopp J., Schroder K. NLRP3 inflammasome activation: the convergence of multiple signalling pathways on ROS production?. Nat. Rev. Immunol. 2010, 10:210-215.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 210-215
    • Tschopp, J.1    Schroder, K.2
  • 14
    • 0346350694 scopus 로고    scopus 로고
    • Cutting edge: CIAS1/cryopyrin/PYPAF1/NALP3/CATERPILLER 1.1 is an inducible inflammatory mediator with NF-kappa B suppressive properties
    • O'Connor W., Harton J.A., Zhu X., Linhoff M.W., Ting J.P. Cutting edge: CIAS1/cryopyrin/PYPAF1/NALP3/CATERPILLER 1.1 is an inducible inflammatory mediator with NF-kappa B suppressive properties. J. Immunol. 2003, 171:6329-6333.
    • (2003) J. Immunol. , vol.171 , pp. 6329-6333
    • O'Connor, W.1    Harton, J.A.2    Zhu, X.3    Linhoff, M.W.4    Ting, J.P.5
  • 16
    • 0035895992 scopus 로고    scopus 로고
    • Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-kappaB
    • Ogura Y., Inohara N., Benito A., Chen F.F., Yamaoka S., Nunez G. Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-kappaB. J. Biol. Chem. 2001, 276:4812-4818.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4812-4818
    • Ogura, Y.1    Inohara, N.2    Benito, A.3    Chen, F.F.4    Yamaoka, S.5    Nunez, G.6
  • 21
  • 23
    • 84856001920 scopus 로고    scopus 로고
    • Mutational analysis of human NOD1 and NOD2 NACHT domains reveals different modes of activation
    • Zurek B., Proell M., Wagner R.N., Schwarzenbacher R., Kufer T.A. Mutational analysis of human NOD1 and NOD2 NACHT domains reveals different modes of activation. Innate Immun. 2012, 18:100-111.
    • (2012) Innate Immun. , vol.18 , pp. 100-111
    • Zurek, B.1    Proell, M.2    Wagner, R.N.3    Schwarzenbacher, R.4    Kufer, T.A.5
  • 27
    • 59649103157 scopus 로고    scopus 로고
    • Wheel of life, wheel of death: a mechanistic insight into signaling by STAND proteins
    • Danot O., Marquenet E., Vidal-Ingigliardi D., Richet E. Wheel of life, wheel of death: a mechanistic insight into signaling by STAND proteins. Structure 2009, 17:172-182.
    • (2009) Structure , vol.17 , pp. 172-182
    • Danot, O.1    Marquenet, E.2    Vidal-Ingigliardi, D.3    Richet, E.4
  • 28
    • 84869044838 scopus 로고    scopus 로고
    • Formation and structure of a NAIP5-NLRC4 inflammasome induced by direct interactions with conserved N- and C-terminal regions of flagellin
    • Halff E.F., Diebolder C.A., Versteeg M., Schouten A., Brondijk T.H., Huizinga E.G. Formation and structure of a NAIP5-NLRC4 inflammasome induced by direct interactions with conserved N- and C-terminal regions of flagellin. J. Biol. Chem. 2012, 287:38460-38472.
    • (2012) J. Biol. Chem. , vol.287 , pp. 38460-38472
    • Halff, E.F.1    Diebolder, C.A.2    Versteeg, M.3    Schouten, A.4    Brondijk, T.H.5    Huizinga, E.G.6
  • 29
    • 84865434771 scopus 로고    scopus 로고
    • The innate immune protein Nod2 binds directly to MDP, a bacterial cell wall fragment
    • Grimes C.L., Ariyananda Lde Z., Melnyk J.E., O'Shea E.K. The innate immune protein Nod2 binds directly to MDP, a bacterial cell wall fragment. J. Am. Chem. Soc. 2012, 134:13535-13537.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 13535-13537
    • Grimes, C.L.1    Ariyananda Lde, Z.2    Melnyk, J.E.3    O'Shea, E.K.4
  • 30
    • 80052230551 scopus 로고    scopus 로고
    • L-Ala-gamma-D-Glu-meso-diaminopimelic acid (DAP) interacts directly with leucine-rich region domain of nucleotide-binding oligomerization domain 1, increasing phosphorylation activity of receptor-interacting serine/threonine-protein kinase 2 and its interaction with nucleotide-binding oligomerization domain 1
    • Laroui H., Yan Y., Narui Y., Ingersoll S.A., Ayyadurai S., Charania M.A., Zhou F., Wang B., Salaita K., Sitaraman S.V., Merlin D. L-Ala-gamma-D-Glu-meso-diaminopimelic acid (DAP) interacts directly with leucine-rich region domain of nucleotide-binding oligomerization domain 1, increasing phosphorylation activity of receptor-interacting serine/threonine-protein kinase 2 and its interaction with nucleotide-binding oligomerization domain 1. J. Biol. Chem. 2011, 286:31003-31013.
    • (2011) J. Biol. Chem. , vol.286 , pp. 31003-31013
    • Laroui, H.1    Yan, Y.2    Narui, Y.3    Ingersoll, S.A.4    Ayyadurai, S.5    Charania, M.A.6    Zhou, F.7    Wang, B.8    Salaita, K.9    Sitaraman, S.V.10    Merlin, D.11
  • 31
    • 84863336565 scopus 로고    scopus 로고
    • Pathogen sensing by nucleotide-binding oligomerization domain-containing protein 2 (NOD2) is mediated by direct binding to muramyl dipeptide and ATP
    • Mo J., Boyle J.P., Howard C.B., Monie T.P., Davis B.K., Duncan J.A. Pathogen sensing by nucleotide-binding oligomerization domain-containing protein 2 (NOD2) is mediated by direct binding to muramyl dipeptide and ATP. J. Biol. Chem. 2012, 287:23057-23067.
    • (2012) J. Biol. Chem. , vol.287 , pp. 23057-23067
    • Mo, J.1    Boyle, J.P.2    Howard, C.B.3    Monie, T.P.4    Davis, B.K.5    Duncan, J.A.6
  • 32
    • 77955091927 scopus 로고    scopus 로고
    • NB-LRR proteins: pairs, pieces, perception, partners, and pathways
    • Eitas T.K., Dangl J.L. NB-LRR proteins: pairs, pieces, perception, partners, and pathways. Curr. Opin. Plant Biol. 2010, 13:472-477.
    • (2010) Curr. Opin. Plant Biol. , vol.13 , pp. 472-477
    • Eitas, T.K.1    Dangl, J.L.2
  • 33
    • 84862901883 scopus 로고    scopus 로고
    • Sensing bacterial infections by NAIP receptors in NLRC4 inflammasome activation
    • Gong Y.N., Shao F. Sensing bacterial infections by NAIP receptors in NLRC4 inflammasome activation. Protein Cell 2012, 3:98-105.
    • (2012) Protein Cell , vol.3 , pp. 98-105
    • Gong, Y.N.1    Shao, F.2
  • 34
    • 84862339477 scopus 로고    scopus 로고
    • NAIPs: building an innate immune barrier against bacterial pathogens. NAIPs function as sensors that initiate innate immunity by detection of bacterial proteins in the host cell cytosol
    • Kofoed E.M., Vance R.E. NAIPs: building an innate immune barrier against bacterial pathogens. NAIPs function as sensors that initiate innate immunity by detection of bacterial proteins in the host cell cytosol. Bioessays 2012, 34:589-598.
    • (2012) Bioessays , vol.34 , pp. 589-598
    • Kofoed, E.M.1    Vance, R.E.2
  • 35
    • 3142674847 scopus 로고    scopus 로고
    • Heterotypic interactions among NACHT domains: implications for regulation of innate immune responses
    • Damiano J.S., Oliveira V., Welsh K., Reed J.C. Heterotypic interactions among NACHT domains: implications for regulation of innate immune responses. Biochem. J. 2004, 381:213-219.
    • (2004) Biochem. J. , vol.381 , pp. 213-219
    • Damiano, J.S.1    Oliveira, V.2    Welsh, K.3    Reed, J.C.4
  • 40
    • 80053379974 scopus 로고    scopus 로고
    • Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
    • Kofoed E.M., Vance R.E. Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity. Nature 2011, 477:592-595.
    • (2011) Nature , vol.477 , pp. 592-595
    • Kofoed, E.M.1    Vance, R.E.2
  • 41
    • 80053349020 scopus 로고    scopus 로고
    • The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus
    • Zhao Y., Yang J., Shi J., Gong Y.N., Lu Q., Xu H., Liu L., Shao F. The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature 2011, 477:596-600.
    • (2011) Nature , vol.477 , pp. 596-600
    • Zhao, Y.1    Yang, J.2    Shi, J.3    Gong, Y.N.4    Lu, Q.5    Xu, H.6    Liu, L.7    Shao, F.8
  • 42
    • 44049099252 scopus 로고    scopus 로고
    • Arabidopsis TAO1 is a TIR-NB-LRR protein that contributes to disease resistance induced by the Pseudomonas syringae effector AvrB
    • Eitas T.K., Nimchuk Z.L., Dangl J.L. Arabidopsis TAO1 is a TIR-NB-LRR protein that contributes to disease resistance induced by the Pseudomonas syringae effector AvrB. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:6475-6480.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 6475-6480
    • Eitas, T.K.1    Nimchuk, Z.L.2    Dangl, J.L.3
  • 43
    • 20144382377 scopus 로고    scopus 로고
    • NRG1, a CC-NB-LRR protein, together with N, a TIR-NB-LRR protein, mediates resistance against tobacco mosaic virus
    • Peart J.R., Mestre P., Lu R., Malcuit I., Baulcombe D.C. NRG1, a CC-NB-LRR protein, together with N, a TIR-NB-LRR protein, mediates resistance against tobacco mosaic virus. Curr. Biol. 2005, 15:968-973.
    • (2005) Curr. Biol. , vol.15 , pp. 968-973
    • Peart, J.R.1    Mestre, P.2    Lu, R.3    Malcuit, I.4    Baulcombe, D.C.5
  • 47
    • 77956103055 scopus 로고    scopus 로고
    • Quantitative expression of RIG-like helicase, NOD-like receptor and inflammasome-related mRNAs in humans and mice
    • Lech M., Avila-Ferrufino A., Skuginna V., Susanti H.E., Anders H.J. Quantitative expression of RIG-like helicase, NOD-like receptor and inflammasome-related mRNAs in humans and mice. Int. Immunol. 2010, 22:717-728.
    • (2010) Int. Immunol. , vol.22 , pp. 717-728
    • Lech, M.1    Avila-Ferrufino, A.2    Skuginna, V.3    Susanti, H.E.4    Anders, H.J.5
  • 51
    • 84859027286 scopus 로고    scopus 로고
    • Functional characterization of the p53 binding site in the human PYNOD promoter
    • Zeng Q., Lu D., Tang Q., Tian L., Wang H., Tang S., Hu C. Functional characterization of the p53 binding site in the human PYNOD promoter. Hum. Immunol. 2012, 73:355-363.
    • (2012) Hum. Immunol. , vol.73 , pp. 355-363
    • Zeng, Q.1    Lu, D.2    Tang, Q.3    Tian, L.4    Wang, H.5    Tang, S.6    Hu, C.7
  • 52
    • 84871955225 scopus 로고    scopus 로고
    • Interactions between the tumor suppressor p53 and immune responses
    • Menendez D., Shatz M., Resnick M.A. Interactions between the tumor suppressor p53 and immune responses. Curr. Opin. Oncol. 2013, 25:85-92.
    • (2013) Curr. Opin. Oncol. , vol.25 , pp. 85-92
    • Menendez, D.1    Shatz, M.2    Resnick, M.A.3
  • 53
    • 64249098607 scopus 로고    scopus 로고
    • Evaluation of Nod-like receptor (NLR) effector domain interactions
    • Wagner R.N., Proell M., Kufer T.A., Schwarzenbacher R. Evaluation of Nod-like receptor (NLR) effector domain interactions. PLoS One 2009, 4:e4931.
    • (2009) PLoS One , vol.4
    • Wagner, R.N.1    Proell, M.2    Kufer, T.A.3    Schwarzenbacher, R.4
  • 55
    • 40049108218 scopus 로고    scopus 로고
    • COPs and POPs: modulators of inflammasome activity
    • Stehlik C., Dorfleutner A. COPs and POPs: modulators of inflammasome activity. J. Immunol. 2007, 179:7993-7998.
    • (2007) J. Immunol. , vol.179 , pp. 7993-7998
    • Stehlik, C.1    Dorfleutner, A.2
  • 56
    • 81755171449 scopus 로고    scopus 로고
    • Uncoupling of pyrin-only protein 2 (POP2)-mediated dual regulation of NF-kappaB and the inflammasome
    • Atianand M.K., Harton J.A. Uncoupling of pyrin-only protein 2 (POP2)-mediated dual regulation of NF-kappaB and the inflammasome. J. Biol. Chem. 2011, 286:40536-40547.
    • (2011) J. Biol. Chem. , vol.286 , pp. 40536-40547
    • Atianand, M.K.1    Harton, J.A.2
  • 57
    • 24044515544 scopus 로고    scopus 로고
    • CATERPILLER 16.2 (CLR16.2), a novel NBD/LRR family member that negatively regulates T cell function
    • Conti B.J., Davis B.K., Zhang J., O'Connor W., Williams K.L., Ting J.P. CATERPILLER 16.2 (CLR16.2), a novel NBD/LRR family member that negatively regulates T cell function. J. Biol. Chem. 2005, 280:18375-18385.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18375-18385
    • Conti, B.J.1    Davis, B.K.2    Zhang, J.3    O'Connor, W.4    Williams, K.L.5    Ting, J.P.6
  • 62
    • 84870212902 scopus 로고    scopus 로고
    • NLRC5: a key regulator of MHC class I-dependent immune responses
    • Kobayashi K.S., van den Elsen P.J. NLRC5: a key regulator of MHC class I-dependent immune responses. Nat. Rev. Immunol. 2012, 12:813-820.
    • (2012) Nat. Rev. Immunol. , vol.12 , pp. 813-820
    • Kobayashi, K.S.1    van den Elsen, P.J.2
  • 66
    • 84877102781 scopus 로고    scopus 로고
    • Beyond pattern recognition: NOD-like receptors in dendritic cells
    • (Epub ahead of print)
    • Krishnaswamy J.K., Chu T., Eisenbarth S.C. Beyond pattern recognition: NOD-like receptors in dendritic cells. Trends Immunol. 2013, (Epub ahead of print). http://dx.doi.org/10.1016/j.it.2012.12.003.
    • (2013) Trends Immunol.
    • Krishnaswamy, J.K.1    Chu, T.2    Eisenbarth, S.C.3
  • 68
    • 83555176154 scopus 로고    scopus 로고
    • Nucleotide-binding oligomerization domain-like receptors and inflammasomes in the pathogenesis of non-microbial inflammation and diseases
    • Mason D.R., Beck P.L., Muruve D.A. Nucleotide-binding oligomerization domain-like receptors and inflammasomes in the pathogenesis of non-microbial inflammation and diseases. J. Innate Immun. 2012, 4:16-30.
    • (2012) J. Innate Immun. , vol.4 , pp. 16-30
    • Mason, D.R.1    Beck, P.L.2    Muruve, D.A.3
  • 72
    • 22244465576 scopus 로고    scopus 로고
    • Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-{kappa}B activation in muramyl dipeptide recognition
    • Barnich N., Aguirre J.E., Reinecker H.C., Xavier R., Podolsky D.K. Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-{kappa}B activation in muramyl dipeptide recognition. J. Cell. Biol. 2005, 170:21-26.
    • (2005) J. Cell. Biol. , vol.170 , pp. 21-26
    • Barnich, N.1    Aguirre, J.E.2    Reinecker, H.C.3    Xavier, R.4    Podolsky, D.K.5
  • 73
    • 38049177193 scopus 로고    scopus 로고
    • The pattern-recognition molecule Nod1 is localized at the plasma membrane at sites of bacterial interaction
    • Kufer T.A., Kremmer E., Adam A.C., Philpott D.J., Sansonetti P.J. The pattern-recognition molecule Nod1 is localized at the plasma membrane at sites of bacterial interaction. Cell. Microbiol. 2008, 10:477-486.
    • (2008) Cell. Microbiol. , vol.10 , pp. 477-486
    • Kufer, T.A.1    Kremmer, E.2    Adam, A.C.3    Philpott, D.J.4    Sansonetti, P.J.5
  • 76
    • 0037452765 scopus 로고    scopus 로고
    • GDE1/MIR16 is a glycerophosphoinositol phosphodiesterase regulated by stimulation of G protein-coupled receptors
    • Zheng B., Berrie C.P., Corda D., Farquhar M.G. GDE1/MIR16 is a glycerophosphoinositol phosphodiesterase regulated by stimulation of G protein-coupled receptors. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:1745-1750.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 1745-1750
    • Zheng, B.1    Berrie, C.P.2    Corda, D.3    Farquhar, M.G.4


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