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Volumn 292, Issue 4, 2017, Pages 1218-1230

A disease-associated mutant of NLRC4 shows enhanced interaction with SUG1 leading to constitutive fadddependent caspase-8 activation and cell death

Author keywords

[No Author keywords available]

Indexed keywords

CELL DEATH; CHEMICAL ACTIVATION; CYTOLOGY; ENZYME ACTIVITY; PHOSPHORYLATION; PROTEINS;

EID: 85019005737     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.763979     Document Type: Article
Times cited : (42)

References (38)
  • 2
    • 80053379974 scopus 로고    scopus 로고
    • Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
    • Kofoed, E. M., and Vance, R. E. (2011) Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity. Nature 477, 592-595
    • (2011) Nature , vol.477 , pp. 592-595
    • Kofoed, E.M.1    Vance, R.E.2
  • 3
    • 84898031590 scopus 로고    scopus 로고
    • Molecular basis for specific recognition of bacterial ligands by NAIP/NLRC4 inflammasomes
    • Tenthorey, J. L., Kofoed, E. M., Daugherty, M. D., Malik, H. S., and Vance, R. E. (2014) Molecular basis for specific recognition of bacterial ligands by NAIP/NLRC4 inflammasomes. Mol. Cell 54, 17-29
    • (2014) Mol. Cell , vol.54 , pp. 17-29
    • Tenthorey, J.L.1    Kofoed, E.M.2    Daugherty, M.D.3    Malik, H.S.4    Vance, R.E.5
  • 4
    • 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., and Shao, F. (2011) The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature 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
  • 6
    • 84949201317 scopus 로고    scopus 로고
    • Cryoelectron tomography of the NAIP5/NLRC4 inflammasome: Implications for NLR activation
    • Diebolder, C. A., Halff, E. F., Koster, A. J., Huizinga, E. G., and Koning, R. I. (2015) Cryoelectron tomography of the NAIP5/NLRC4 inflammasome: implications for NLR activation. Structure 23, 2349-2357
    • (2015) Structure , vol.23 , pp. 2349-2357
    • Diebolder, C.A.1    Halff, E.F.2    Koster, A.J.3    Huizinga, E.G.4    Koning, R.I.5
  • 12
    • 84902588358 scopus 로고    scopus 로고
    • NLRC4 expression in intestinal epithelial cells mediates protection against an enteric pathogen
    • Nordlander, S., Pott, J., and Maloy, K. J. (2014) NLRC4 expression in intestinal epithelial cells mediates protection against an enteric pathogen. Mucosal Immunol. 7, 775-785
    • (2014) Mucosal Immunol. , vol.7 , pp. 775-785
    • Nordlander, S.1    Pott, J.2    Maloy, K.J.3
  • 13
    • 84908024529 scopus 로고    scopus 로고
    • Epithelium-intrinsic NAIP/NLRC4 inflammasome drives infected enterocyte expulsion to restrict Salmonella replication in the intestinal mucosa
    • Sellin, M. E., Müller, A. A., Felmy, B., Dolowschiak, T., Diard, M., Tardivel, A., Maslowski, K. M., and Hardt, W. D. (2014) Epithelium-intrinsic NAIP/NLRC4 inflammasome drives infected enterocyte expulsion to restrict Salmonella replication in the intestinal mucosa. Cell Host Microbe 16, 237-248
    • (2014) Cell Host Microbe , vol.16 , pp. 237-248
    • Sellin, M.E.1    Müller, A.A.2    Felmy, B.3    Dolowschiak, T.4    Diard, M.5    Tardivel, A.6    Maslowski, K.M.7    Hardt, W.D.8
  • 14
    • 84944278525 scopus 로고    scopus 로고
    • Differential expression of inflammasomes in lung cancer cell lines and tissues
    • Kong, H., Wang, Y., Zeng, X., Wang, Z., Wang, H., and Xie, W. (2015) Differential expression of inflammasomes in lung cancer cell lines and tissues. Tumour Biol. 36, 7501-7513
    • (2015) Tumour Biol. , vol.36 , pp. 7501-7513
    • Kong, H.1    Wang, Y.2    Zeng, X.3    Wang, Z.4    Wang, H.5    Xie, W.6
  • 15
    • 77950887181 scopus 로고    scopus 로고
    • Interaction with Sug1 enables Ipaf ubiquitination leading to caspase 8 activation and cell death
    • Kumar, Y., Radha, V., and Swarup, G. (2010) Interaction with Sug1 enables Ipaf ubiquitination leading to caspase 8 activation and cell death. Biochem. J. 427, 91-104
    • (2010) Biochem. J. , vol.427 , pp. 91-104
    • Kumar, Y.1    Radha, V.2    Swarup, G.3
  • 18
    • 84911922142 scopus 로고    scopus 로고
    • An inherited mutation in NLRC4 causes autoinflammation in human and mice
    • Kitamura, A., Sasaki, Y., Abe, T., Kano, H., and Yasutomo, K. (2014) An inherited mutation in NLRC4 causes autoinflammation in human and mice. J. Exp. Med. 211, 2385-2396
    • (2014) J. Exp. Med. , vol.211 , pp. 2385-2396
    • Kitamura, A.1    Sasaki, Y.2    Abe, T.3    Kano, H.4    Yasutomo, K.5
  • 20
    • 40149102342 scopus 로고    scopus 로고
    • The 19S proteasome ATPase Sug1 plays a critical role in regulating MHC class II transcription
    • Bhat, K. P., Turner, J. D., Myers, S. E., Cape, A. D., Ting, J. P., and Greer, S. F. (2008) The 19S proteasome ATPase Sug1 plays a critical role in regulating MHC class II transcription. Mol. Immunol. 45, 2214-2224
    • (2008) Mol. Immunol. , vol.45 , pp. 2214-2224
    • Bhat, K.P.1    Turner, J.D.2    Myers, S.E.3    Cape, A.D.4    Ting, J.P.5    Greer, S.F.6
  • 21
    • 84928106003 scopus 로고    scopus 로고
    • The 26S proteasome and initiation of gene transcription
    • Durairaj, G., and Kaiser, P. (2014) The 26S proteasome and initiation of gene transcription. Biomolecules 4, 827-847
    • (2014) Biomolecules , vol.4 , pp. 827-847
    • Durairaj, G.1    Kaiser, P.2
  • 22
    • 27844442187 scopus 로고    scopus 로고
    • TRAF6-mediated ubiquitination regulates nuclear translocation of NRIF, the p75 receptor interactor
    • Geetha, T., Kenchappa, R. S., Wooten, M. W., and Carter, B. D. (2005) TRAF6-mediated ubiquitination regulates nuclear translocation of NRIF, the p75 receptor interactor. EMBO J. 24, 3859-3868
    • (2005) EMBO J. , vol.24 , pp. 3859-3868
    • Geetha, T.1    Kenchappa, R.S.2    Wooten, M.W.3    Carter, B.D.4
  • 24
    • 84887439544 scopus 로고    scopus 로고
    • Salmonella infection induces recruitment of Caspase-8 to the inflammasome to modulate IL-1β production
    • Man, S. M., Tourlomousis, P., Hopkins, L., Monie, T. P., Fitzgerald, K. A., and Bryant, C. E. (2013) Salmonella infection induces recruitment of Caspase-8 to the inflammasome to modulate IL-1β production. J. Immunol. 191, 5239-5246
    • (2013) J. Immunol. , vol.191 , pp. 5239-5246
    • Man, S.M.1    Tourlomousis, P.2    Hopkins, L.3    Monie, T.P.4    Fitzgerald, K.A.5    Bryant, C.E.6
  • 29
    • 13244252271 scopus 로고    scopus 로고
    • Caspase-1 activator Ipaf is a p53-inducible gene involved in apoptosis
    • Sadasivam, S., Gupta, S., Radha, V., Batta, K., Kundu, T. K., and Swarup, G. (2005) Caspase-1 activator Ipaf is a p53-inducible gene involved in apoptosis. Oncogene 24, 627-636
    • (2005) Oncogene , vol.24 , pp. 627-636
    • Sadasivam, S.1    Gupta, S.2    Radha, V.3    Batta, K.4    Kundu, T.K.5    Swarup, G.6
  • 30
    • 33745211768 scopus 로고    scopus 로고
    • Involvement of caspase 1 and its activator Ipaf upstream of mitochondrial events in apoptosis
    • Thalappilly, S., Sadasivam, S., Radha, V., and Swarup, G. (2006) Involvement of caspase 1 and its activator Ipaf upstream of mitochondrial events in apoptosis. FEBS J. 273, 2766-2778
    • (2006) FEBS J. , vol.273 , pp. 2766-2778
    • Thalappilly, S.1    Sadasivam, S.2    Radha, V.3    Swarup, G.4
  • 35
    • 77954620472 scopus 로고    scopus 로고
    • FADD: A regulator of life and death
    • Tourneur, L., and Chiocchia, G. (2010) FADD: a regulator of life and death. Trends Immunol. 31, 260-269
    • (2010) Trends Immunol. , vol.31 , pp. 260-269
    • Tourneur, L.1    Chiocchia, G.2
  • 36
    • 65549160961 scopus 로고    scopus 로고
    • The CULt of caspase-8 ubiquitination
    • Békés, M., and Salvesen, G. S. (2009) The CULt of caspase-8 ubiquitination. Cell 137, 604-606
    • (2009) Cell , vol.137 , pp. 604-606
    • Békés, M.1    Salvesen, G.S.2
  • 37
    • 0346101792 scopus 로고    scopus 로고
    • Physical and functional interaction between Hck tyrosine kinase and guanine nucleotide exchange factor C3G results in apoptosis, which is independent of C3G catalytic domain
    • Shivakrupa, R., Radha, V., Sudhakar, C., and Swarup, G. (2003) Physical and functional interaction between Hck tyrosine kinase and guanine nucleotide exchange factor C3G results in apoptosis, which is independent of C3G catalytic domain. J. Biol. Chem. 278, 52188-52194
    • (2003) J. Biol. Chem. , vol.278 , pp. 52188-52194
    • Shivakrupa, R.1    Radha, V.2    Sudhakar, C.3    Swarup, G.4
  • 38
    • 0036016916 scopus 로고    scopus 로고
    • Induction of cytochrome c release and apoptosis by Hck-SH3 domain-mediated signalling requires caspase-3
    • Radha, V., Sudhakar, C., Ray, P., and Swarup, G. (2002) Induction of cytochrome c release and apoptosis by Hck-SH3 domain-mediated signalling requires caspase-3. Apoptosis 7, 195-207
    • (2002) Apoptosis , vol.7 , pp. 195-207
    • Radha, V.1    Sudhakar, C.2    Ray, P.3    Swarup, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.