메뉴 건너뛰기




Volumn 1863, Issue 12, 2016, Pages 3148-3159

Corrigendum to “Yersinia YopJ negatively regulates IRF3-mediated antibacterial response through disruption of STING-mediated cytosolic DNA signaling” [Biochim. Biophys. Acta 1863 (12) (2016) 3148–3159] (S0167488916302580) (10.1016/j.bbamcr.2016.10.004));Yersinia YopJ negatively regulates IRF3-mediated antibacterial response through disruption of STING-mediated cytosolic DNA signaling

Author keywords

Deubiquitination; IFN ; IRF3; STING; Yop J

Indexed keywords

ADAPTOR PROTEIN; BACTERIAL ENZYME; CYSTEINE; CYSTEINE PROTEINASE; DNA; GAMMA INTERFERON; INTERFERON REGULATORY FACTOR 3; PHOSPHOTRANSFERASE; STIMULATOR OF INTERFERON GENE PROTEIN; TANK BINDING KINASE 1; UNCLASSIFIED DRUG; YERSINIA OUTER PROTEIN J; BACTERIAL PROTEIN; BETA INTERFERON; IRF3 PROTEIN, MOUSE; MEMBRANE PROTEIN; MPYS PROTEIN, MOUSE; PROTEIN SERINE THREONINE KINASE; TBK1 PROTEIN, MOUSE; YOPP PROTEIN, YERSINIA;

EID: 84992025599     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2017.07.018     Document Type: Erratum
Times cited : (12)

References (39)
  • 1
    • 78149233514 scopus 로고    scopus 로고
    • The innate immune system in the intestine
    • [1] Uematsu, S., Fujimoto, K., The innate immune system in the intestine. Microbiol. Immunol. 54 (2010), 645–657.
    • (2010) Microbiol. Immunol. , vol.54 , pp. 645-657
    • Uematsu, S.1    Fujimoto, K.2
  • 2
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • [2] Akira, S., Uematsu, S., Takeuchi, O., Pathogen recognition and innate immunity. Cell 124 (2006), 783–801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 3
    • 84918775897 scopus 로고    scopus 로고
    • MITA/STING: a central and multifaceted mediator in innate immune response
    • [3] Ran, Y., Shu, H.B., Wang, Y.Y., MITA/STING: a central and multifaceted mediator in innate immune response. Cytokine Growth Factor Rev. 25 (2014), 631–639.
    • (2014) Cytokine Growth Factor Rev. , vol.25 , pp. 631-639
    • Ran, Y.1    Shu, H.B.2    Wang, Y.Y.3
  • 7
    • 78650214109 scopus 로고    scopus 로고
    • The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA
    • [7] Tsuchida, T., Zou, J., Saitoh, T., Kumar, H., Abe, T., Matsuura, Y., Kawai, T., Akira, S., The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA. Immunity 33 (2010), 765–776.
    • (2010) Immunity , vol.33 , pp. 765-776
    • Tsuchida, T.1    Zou, J.2    Saitoh, T.3    Kumar, H.4    Abe, T.5    Matsuura, Y.6    Kawai, T.7    Akira, S.8
  • 8
    • 84865270570 scopus 로고    scopus 로고
    • TRIM32 protein modulates type I interferon induction and cellular antiviral response by targeting MITA/STING protein for K63-linked ubiquitination
    • [8] Zhang, J., Hu, M.M., Wang, Y.Y., Shu, H.B., TRIM32 protein modulates type I interferon induction and cellular antiviral response by targeting MITA/STING protein for K63-linked ubiquitination. J. Biol. Chem. 287 (2012), 28646–28655.
    • (2012) J. Biol. Chem. , vol.287 , pp. 28646-28655
    • Zhang, J.1    Hu, M.M.2    Wang, Y.Y.3    Shu, H.B.4
  • 9
    • 84959353023 scopus 로고    scopus 로고
    • STING activation by translocation from the ER is associated with infection and autoinflammatory disease
    • [9] Dobbs, N., Burnaevskiy, N., Chen, D., Gonugunta, V.K., Alto, N.M., Yan, N., STING activation by translocation from the ER is associated with infection and autoinflammatory disease. Cell Host Microbe 18 (2015), 157–168.
    • (2015) Cell Host Microbe , vol.18 , pp. 157-168
    • Dobbs, N.1    Burnaevskiy, N.2    Chen, D.3    Gonugunta, V.K.4    Alto, N.M.5    Yan, N.6
  • 11
    • 53349178089 scopus 로고    scopus 로고
    • STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
    • [11] Ishikawa, H., Barber, G.N., STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling. Nature 455 (2008), 674–678.
    • (2008) Nature , vol.455 , pp. 674-678
    • Ishikawa, H.1    Barber, G.N.2
  • 12
    • 53349168904 scopus 로고    scopus 로고
    • The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation
    • [12] Zhong, B., Yang, Y., Li, S., Wang, Y.Y., Li, Y., Diao, F., Lei, C., He, X., Zhang, L., Tien, P., Shu, H.B., The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation. Immunity 29 (2008), 538–550.
    • (2008) Immunity , vol.29 , pp. 538-550
    • Zhong, B.1    Yang, Y.2    Li, S.3    Wang, Y.Y.4    Li, Y.5    Diao, F.6    Lei, C.7    He, X.8    Zhang, L.9    Tien, P.10    Shu, H.B.11
  • 13
    • 70349943834 scopus 로고    scopus 로고
    • STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity
    • [13] Ishikawa, H., Ma, Z., Barber, G.N., STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity. Nature 461 (2009), 788–792.
    • (2009) Nature , vol.461 , pp. 788-792
    • Ishikawa, H.1    Ma, Z.2    Barber, G.N.3
  • 14
    • 84857937262 scopus 로고    scopus 로고
    • STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway
    • (ra20)
    • [14] Tanaka, Y., Chen, Z.J., STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway. Sci. Signal., 5, 2012 (ra20).
    • (2012) Sci. Signal. , vol.5
    • Tanaka, Y.1    Chen, Z.J.2
  • 16
    • 25444476788 scopus 로고    scopus 로고
    • Yersinia outer proteins: role in modulation of host cell signaling responses and pathogenesis
    • [16] Viboud, G.I., Bliska, J.B., Yersinia outer proteins: role in modulation of host cell signaling responses and pathogenesis. Annu. Rev. Microbiol. 59 (2005), 69–89.
    • (2005) Annu. Rev. Microbiol. , vol.59 , pp. 69-89
    • Viboud, G.I.1    Bliska, J.B.2
  • 18
    • 33744457909 scopus 로고    scopus 로고
    • Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation
    • [18] Mukherjee, S., Keitany, G., Li, Y., Wang, Y., Ball, H.L., Goldsmith, E.J., Orth, K., Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation. Science 312 (2006), 1211–1214.
    • (2006) Science , vol.312 , pp. 1211-1214
    • Mukherjee, S.1    Keitany, G.2    Li, Y.3    Wang, Y.4    Ball, H.L.5    Goldsmith, E.J.6    Orth, K.7
  • 20
    • 27944471038 scopus 로고    scopus 로고
    • Yersinia virulence factor YopJ acts as a deubiquitinase to inhibit NF-kappa B activation
    • [20] Zhou, H., Monack, D.M., Kayagaki, N., Wertz, I., Yin, J., Wolf, B., Dixit, V.M., Yersinia virulence factor YopJ acts as a deubiquitinase to inhibit NF-kappa B activation. J. Exp. Med. 202 (2005), 1327–1332.
    • (2005) J. Exp. Med. , vol.202 , pp. 1327-1332
    • Zhou, H.1    Monack, D.M.2    Kayagaki, N.3    Wertz, I.4    Yin, J.5    Wolf, B.6    Dixit, V.M.7
  • 24
    • 84957658198 scopus 로고    scopus 로고
    • Bacterial E3 ubiquitin ligase IpaH4.5 of Shigella flexneri targets TBK1 to dampen the host antibacterial response
    • [24] Zheng, Z., Wei, C., Guan, K., Yuan, Y., Zhang, Y., Ma, S., Cao, Y., Wang, F., Zhong, H., He, X., Bacterial E3 ubiquitin ligase IpaH4.5 of Shigella flexneri targets TBK1 to dampen the host antibacterial response. J. Immunol. 196 (2016), 1199–1208.
    • (2016) J. Immunol. , vol.196 , pp. 1199-1208
    • Zheng, Z.1    Wei, C.2    Guan, K.3    Yuan, Y.4    Zhang, Y.5    Ma, S.6    Cao, Y.7    Wang, F.8    Zhong, H.9    He, X.10
  • 25
    • 84864606633 scopus 로고    scopus 로고
    • Opposing roles for interferon regulatory factor-3 (IRF-3) and type I interferon signaling during plague
    • e1002817
    • [25] Patel, A.A., Lee-Lewis, H., Hughes-Hanks, J., Lewis, C.A., Anderson, D.M., Opposing roles for interferon regulatory factor-3 (IRF-3) and type I interferon signaling during plague. PLoS Pathog., 8, 2012, e1002817.
    • (2012) PLoS Pathog. , vol.8
    • Patel, A.A.1    Lee-Lewis, H.2    Hughes-Hanks, J.3    Lewis, C.A.4    Anderson, D.M.5
  • 26
    • 34848831208 scopus 로고    scopus 로고
    • YopJ targets TRAF proteins to inhibit TLR-mediated NF-kappaB, MAPK and IRF3 signal transduction
    • [26] Sweet, C.R., Conlon, J., Golenbock, D.T., Goguen, J., Silverman, N., YopJ targets TRAF proteins to inhibit TLR-mediated NF-kappaB, MAPK and IRF3 signal transduction. Cell. Microbiol. 9 (2007), 2700–2715.
    • (2007) Cell. Microbiol. , vol.9 , pp. 2700-2715
    • Sweet, C.R.1    Conlon, J.2    Golenbock, D.T.3    Goguen, J.4    Silverman, N.5
  • 29
    • 84870520072 scopus 로고    scopus 로고
    • Trafficking defects in WASH-knockout fibroblasts originate from collapsed endosomal and lysosomal networks
    • [29] Gomez, T.S., Gorman, J.A., de Narvajas, A.A., Koenig, A.O., Billadeau, D.D., Trafficking defects in WASH-knockout fibroblasts originate from collapsed endosomal and lysosomal networks. Mol. Biol. Cell 23 (2012), 3215–3228.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3215-3228
    • Gomez, T.S.1    Gorman, J.A.2    de Narvajas, A.A.3    Koenig, A.O.4    Billadeau, D.D.5
  • 30
    • 77951877953 scopus 로고    scopus 로고
    • Identification and functions of pattern-recognition receptors
    • [30] Kumagai, Y., Akira, S., Identification and functions of pattern-recognition receptors. J. Allergy Clin. Immunol. 125 (2010), 985–992.
    • (2010) J. Allergy Clin. Immunol. , vol.125 , pp. 985-992
    • Kumagai, Y.1    Akira, S.2
  • 31
    • 66549126665 scopus 로고    scopus 로고
    • Yersinia pestis can reside in autophagosomes and avoid xenophagy in murine macrophages by preventing vacuole acidification
    • [31] Pujol, C., Klein, K.A., Romanov, G.A., Palmer, L.E., Cirota, C., Zhao, Z., Bliska, J.B., Yersinia pestis can reside in autophagosomes and avoid xenophagy in murine macrophages by preventing vacuole acidification. Infect. Immun. 77 (2009), 2251–2261.
    • (2009) Infect. Immun. , vol.77 , pp. 2251-2261
    • Pujol, C.1    Klein, K.A.2    Romanov, G.A.3    Palmer, L.E.4    Cirota, C.5    Zhao, Z.6    Bliska, J.B.7
  • 32
    • 62049084519 scopus 로고    scopus 로고
    • The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA
    • [32] Zhong, B., Zhang, L., Lei, C., Li, Y., Mao, A.P., Yang, Y., Wang, Y.Y., Zhang, X.L., Shu, H.B., The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA. Immunity 30 (2009), 397–407.
    • (2009) Immunity , vol.30 , pp. 397-407
    • Zhong, B.1    Zhang, L.2    Lei, C.3    Li, Y.4    Mao, A.P.5    Yang, Y.6    Wang, Y.Y.7    Zhang, X.L.8    Shu, H.B.9
  • 33
    • 84936757319 scopus 로고    scopus 로고
    • TRIM30alpha is a negative-feedback regulator of the intracellular DNA and DNA virus-triggered response by targeting STING
    • e1005012
    • [33] Wang, Y., Lian, Q., Yang, B., Yan, S., Zhou, H., He, L., Lin, G., Lian, Z., Jiang, Z., Sun, B., TRIM30alpha is a negative-feedback regulator of the intracellular DNA and DNA virus-triggered response by targeting STING. PLoS Pathog., 11, 2015, e1005012.
    • (2015) PLoS Pathog. , vol.11
    • Wang, Y.1    Lian, Q.2    Yang, B.3    Yan, S.4    Zhou, H.5    He, L.6    Lin, G.7    Lian, Z.8    Jiang, Z.9    Sun, B.10
  • 34
    • 84982787957 scopus 로고    scopus 로고
    • The endothelial E3 ligase HECW2 promotes endothelial cell junctions by increasing AMOTL1 protein stability via K63-linked ubiquitination
    • [34] Choi, K.S., Choi, H.J., Lee, J.K., Im, S., Zhang, H., Jeong, Y., Park, J.A., Lee, I.K., Kim, Y.M., Kwon, Y.G., The endothelial E3 ligase HECW2 promotes endothelial cell junctions by increasing AMOTL1 protein stability via K63-linked ubiquitination. Cell. Signal. 28 (2016), 1642–1651.
    • (2016) Cell. Signal. , vol.28 , pp. 1642-1651
    • Choi, K.S.1    Choi, H.J.2    Lee, J.K.3    Im, S.4    Zhang, H.5    Jeong, Y.6    Park, J.A.7    Lee, I.K.8    Kim, Y.M.9    Kwon, Y.G.10
  • 35
    • 1342292545 scopus 로고    scopus 로고
    • The yersiniae–a model genus to study the rapid evolution of bacterial pathogens
    • [35] Wren, B.W., The yersiniae–a model genus to study the rapid evolution of bacterial pathogens. Nat. Rev. Microbiol. 1 (2003), 55–64.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 55-64
    • Wren, B.W.1
  • 36
    • 1342344906 scopus 로고    scopus 로고
    • Characterization of oral Yersinia enterocolitica infection in three different strains of inbred mice
    • [36] Handley, S.A., Dube, P.H., Revell, P.A., Miller, V.L., Characterization of oral Yersinia enterocolitica infection in three different strains of inbred mice. Infect. Immun. 72 (2004), 1645–1656.
    • (2004) Infect. Immun. , vol.72 , pp. 1645-1656
    • Handley, S.A.1    Dube, P.H.2    Revell, P.A.3    Miller, V.L.4
  • 37
    • 44949187452 scopus 로고    scopus 로고
    • Reduced secretion of YopJ by Yersinia limits in vivo cell death but enhances bacterial virulence
    • e1000067
    • [37] Brodsky, I.E., Medzhitov, R., Reduced secretion of YopJ by Yersinia limits in vivo cell death but enhances bacterial virulence. PLoS Pathog., 4, 2008, e1000067.
    • (2008) PLoS Pathog. , vol.4
    • Brodsky, I.E.1    Medzhitov, R.2
  • 38
    • 0031744367 scopus 로고    scopus 로고
    • Yersinia-induced apoptosis in vivo aids in the establishment of a systemic infection of mice
    • [38] Monack, D.M., Mecsas, J., Bouley, D., Falkow, S., Yersinia-induced apoptosis in vivo aids in the establishment of a systemic infection of mice. J. Exp. Med. 188 (1998), 2127–2137.
    • (1998) J. Exp. Med. , vol.188 , pp. 2127-2137
    • Monack, D.M.1    Mecsas, J.2    Bouley, D.3    Falkow, S.4
  • 39
    • 33748045153 scopus 로고    scopus 로고
    • Yersinia pestis YopJ suppresses tumor necrosis factor alpha induction and contributes to apoptosis of immune cells in the lymph node but is not required for virulence in a rat model of bubonic plague
    • [39] Lemaitre, N., Sebbane, F., Long, D., Hinnebusch, B.J., Yersinia pestis YopJ suppresses tumor necrosis factor alpha induction and contributes to apoptosis of immune cells in the lymph node but is not required for virulence in a rat model of bubonic plague. Infect. Immun. 74 (2006), 5126–5131.
    • (2006) Infect. Immun. , vol.74 , pp. 5126-5131
    • Lemaitre, N.1    Sebbane, F.2    Long, D.3    Hinnebusch, B.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.