메뉴 건너뛰기




Volumn 111, Issue 4, 2014, Pages 1509-1514

TRIM38 inhibits TNFα- and IL-1β-triggered NF-κB activation by mediating lysosome-dependent degradation of TAB2/3

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; GAMMA INTERFERON; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON REGULATORY FACTOR 1; INTERLEUKIN 1BETA; INTERLEUKIN 6; INTERLEUKIN 8; TAB 2 3 PROTEIN; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; TRIPARTITE MOTIF PROTEIN 38; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR ALPHA INHIBITOR; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84893393844     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1318227111     Document Type: Article
Times cited : (111)

References (25)
  • 1
    • 79651473582 scopus 로고    scopus 로고
    • NF-κB in immunobiology
    • Hayden MS, Ghosh S (2011) NF-κB in immunobiology. Cell Res 21(2):223-244.
    • (2011) Cell Res , vol.21 , Issue.2 , pp. 223-244
    • Hayden, M.S.1    Ghosh, S.2
  • 2
    • 84856641109 scopus 로고    scopus 로고
    • NF-κB the first quarter-century: Remarkable progress and outstanding questions
    • Hayden MS, Ghosh S (2012) NF-κB, the first quarter-century: Remarkable progress and outstanding questions. Genes Dev 26(3):203-234.
    • (2012) Genes Dev , vol.26 , Issue.3 , pp. 203-234
    • Hayden, M.S.1    Ghosh, S.2
  • 3
    • 79551718724 scopus 로고    scopus 로고
    • NF-kappaB: Much learned, much to learn
    • Razani B, Cheng G (2010) NF-kappaB: Much learned, much to learn. Sci Signal 3(138): pe29.
    • (2010) Sci Signal , vol.3 , Issue.138
    • Razani, B.1    Cheng, G.2
  • 4
    • 80051987703 scopus 로고    scopus 로고
    • Crosstalk in NF-κB signaling pathways
    • Oeckinghaus A, Hayden MS, Ghosh S (2011) Crosstalk in NF-κB signaling pathways. Nat Immunol 12(8):695-708.
    • (2011) Nat Immunol , vol.12 , Issue.8 , pp. 695-708
    • Oeckinghaus, A.1    Hayden, M.S.2    Ghosh, S.3
  • 5
    • 53049104824 scopus 로고    scopus 로고
    • TLR-4, IL-1R and TNF-R signaling to NF-kappaB: Variations on a common theme
    • Verstrepen L, et al. (2008) TLR-4, IL-1R and TNF-R signaling to NF-kappaB: Variations on a common theme. Cell Mol Life Sci 65(19):2964-2978.
    • (2008) Cell Mol Life Sci , vol.65 , Issue.19 , pp. 2964-2978
    • Verstrepen, L.1
  • 6
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signalling in the NF-kappaB pathway
    • Chen ZJ (2005) Ubiquitin signalling in the NF-kappaB pathway. Nat Cell Biol 7(8):758-765.
    • (2005) Nat Cell Biol , vol.7 , Issue.8 , pp. 758-765
    • Chen, Z.J.1
  • 8
    • 84865562042 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase MARCH8 negatively regulates IL-1β-induced NF-κB activation by targeting the IL1RAP coreceptor for ubiquitination and degradation
    • Chen R, Li M, Zhang Y, Zhou Q, Shu HB (2012) The E3 ubiquitin ligase MARCH8 negatively regulates IL-1β-induced NF-κB activation by targeting the IL1RAP coreceptor for ubiquitination and degradation. Proc Natl Acad Sci USA 109(35):14128-14133.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.35 , pp. 14128-14133
    • Chen, R.1    Li, M.2    Zhang, Y.3    Zhou, Q.4    Shu, H.B.5
  • 9
    • 50149121101 scopus 로고    scopus 로고
    • Both cIAP1 and cIAP2 regulate TNFalpha-mediated NFkappaB activation
    • Mahoney DJ, et al. (2008) Both cIAP1 and cIAP2 regulate TNFalpha-mediated NFkappaB activation. Proc Natl Acad Sci USA 105(33):11778-11783.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.33 , pp. 11778-11783
    • Mahoney, D.J.1
  • 10
    • 34447118188 scopus 로고    scopus 로고
    • RBCK1 negatively regulates tumor necrosis factor- and interleukin- 1-triggered NF-kappaB activation by targeting TAB2/3 for degradation
    • Tian Y, et al. (2007) RBCK1 negatively regulates tumor necrosis factor- and interleukin- 1-triggered NF-kappaB activation by targeting TAB2/3 for degradation. J Biol Chem 282(23):16776-16782.
    • (2007) J Biol Chem , vol.282 , Issue.23 , pp. 16776-16782
    • Tian, Y.1
  • 11
    • 80255137005 scopus 로고    scopus 로고
    • Rhesus monkey TRIM5α represses HIV-1 LTR promoter activity by negatively regulating TAK1/TAB1/TAB2/TAB3-complex- mediated NF-κB activation
    • Gong J, Shen XH, Qiu H, Chen C, Yang RG (2011) Rhesus monkey TRIM5α represses HIV-1 LTR promoter activity by negatively regulating TAK1/TAB1/TAB2/TAB3-complex- mediated NF-κB activation. Arch Virol 156(11):1997-2006.
    • (2011) Arch Virol , vol.156 , Issue.11 , pp. 1997-2006
    • Gong, J.1    Shen, X.H.2    Qiu, H.3    Chen, C.4    Yang, R.G.5
  • 12
    • 0032939356 scopus 로고    scopus 로고
    • The cytokine-inducible zinc finger protein A20 inhibits IL-1-induced NF-kappaB activation at the level of TRAF6
    • Heyninck K, Beyaert R (1999) The cytokine-inducible zinc finger protein A20 inhibits IL-1-induced NF-kappaB activation at the level of TRAF6. FEBS Lett 442(2-3):147-150.
    • (1999) FEBS Lett , vol.442 , Issue.2-3 , pp. 147-150
    • Heyninck, K.1    Beyaert, R.2
  • 13
    • 84874332545 scopus 로고    scopus 로고
    • USP2a negatively regulates IL-1β- and virus-induced NF-κB activation by deubiquitinating TRAF6
    • He X, et al. (2013) USP2a negatively regulates IL-1β- and virus-induced NF-κB activation by deubiquitinating TRAF6. J Mol Cell Biol 5(1):39-47.
    • (2013) J Mol Cell Biol , vol.5 , Issue.1 , pp. 39-47
    • He, X.1
  • 14
    • 84862907678 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 4 (USP4) targets TRAF2 and TRAF6 for deubiquitination and inhibits TNFα-induced cancer cell migration
    • Xiao N, et al. (2012) Ubiquitin-specific protease 4 (USP4) targets TRAF2 and TRAF6 for deubiquitination and inhibits TNFα-induced cancer cell migration. Biochem J 441(3): 979-986.
    • (2012) Biochem J , vol.441 , Issue.3 , pp. 979-986
    • Xiao, N.1
  • 15
    • 80052049291 scopus 로고    scopus 로고
    • Ubiquitin-specific peptidase 20 targets TRAF6 and human T cell leukemia virus type 1 tax to negatively regulate NF-kappaB signaling
    • Yasunaga J, Lin FC, Lu X, Jeang KT (2011) Ubiquitin-specific peptidase 20 targets TRAF6 and human T cell leukemia virus type 1 tax to negatively regulate NF-kappaB signaling. J Virol 85(13):6212-6219.
    • (2011) J Virol , vol.85 , Issue.13 , pp. 6212-6219
    • Yasunaga, J.1    Lin, F.C.2    Lu, X.3    Jeang, K.T.4
  • 16
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • Trompouki E, et al. (2003) CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Nature 424(6950):793-796.
    • (2003) Nature , vol.424 , Issue.6950 , pp. 793-796
    • Trompouki, E.1
  • 17
    • 4444349272 scopus 로고    scopus 로고
    • The CAP-Gly domain of CYLD associates with the proline-rich sequence in NEMO/IKKgamma
    • Saito K, et al. (2004) The CAP-Gly domain of CYLD associates with the proline-rich sequence in NEMO/IKKgamma. Structure 12(9):1719-1728.
    • (2004) Structure , vol.12 , Issue.9 , pp. 1719-1728
    • Saito, K.1
  • 18
    • 80052691620 scopus 로고    scopus 로고
    • USP4 targets TAK1 to downregulate TNFα-induced NF-κB activation
    • Fan YH, et al. (2011) USP4 targets TAK1 to downregulate TNFα-induced NF-κB activation. Cell Death Differ 18(10):1547-1560.
    • (2011) Cell Death Differ , vol.18 , Issue.10 , pp. 1547-1560
    • Fan, Y.H.1
  • 19
    • 43049152912 scopus 로고    scopus 로고
    • TNF-alpha induces two distinct caspase-8 activation pathways
    • Wang L, Du F, Wang X (2008) TNF-alpha induces two distinct caspase-8 activation pathways. Cell 133(4):693-703.
    • (2008) Cell , vol.133 , Issue.4 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 20
    • 84872358122 scopus 로고    scopus 로고
    • The dual-specificity phosphatase DUSP14 negatively regulates tumor necrosis factor- and interleukin-1-induced nuclear factor-κB activation by dephosphorylating the protein kinase TAK1
    • Zheng H, et al. (2013) The dual-specificity phosphatase DUSP14 negatively regulates tumor necrosis factor- and interleukin-1-induced nuclear factor-κB activation by dephosphorylating the protein kinase TAK1. J Biol Chem 288(2):819-825.
    • (2013) J Biol Chem , vol.288 , Issue.2 , pp. 819-825
    • Zheng, H.1
  • 21
    • 84871946152 scopus 로고    scopus 로고
    • TRIM protein-mediated regulation of inflammatory and innate immune signaling and its association with antiretroviral activity
    • Uchil PD, et al. (2013) TRIM protein-mediated regulation of inflammatory and innate immune signaling and its association with antiretroviral activity. J Virol 87(1):257-272.
    • (2013) J Virol , vol.87 , Issue.1 , pp. 257-272
    • Uchil, P.D.1
  • 22
    • 84862102052 scopus 로고    scopus 로고
    • Tripartite motif-containing protein 38 negatively regulates TLR3/4- and RIG-I-mediated IFN-β production and antiviral response by targeting NAP1
    • Zhao W, et al. (2012) Tripartite motif-containing protein 38 negatively regulates TLR3/4- and RIG-I-mediated IFN-β production and antiviral response by targeting NAP1. J Immunol 188(11):5311-5318.
    • (2012) J Immunol , vol.188 , Issue.11 , pp. 5311-5318
    • Zhao, W.1
  • 23
    • 84863229333 scopus 로고    scopus 로고
    • E3 ubiquitin ligase tripartite motif 38 negatively regulates TLR-mediated immune responses by proteasomal degradation of TNF receptor-associated factor 6 in macrophages
    • Zhao W, Wang L, Zhang M, Yuan C, Gao C (2012) E3 ubiquitin ligase tripartite motif 38 negatively regulates TLR-mediated immune responses by proteasomal degradation of TNF receptor-associated factor 6 in macrophages. J Immunol 188(6):2567-2574.
    • (2012) J Immunol , vol.188 , Issue.6 , pp. 2567-2574
    • Zhao, W.1    Wang, L.2    Zhang, M.3    Yuan, C.4    Gao, C.5
  • 24
    • 84867308377 scopus 로고    scopus 로고
    • TRIM38 negatively regulates TLR3-mediated IFN-β signaling by targeting TRIF for degradation
    • Xue Q, et al. (2012) TRIM38 negatively regulates TLR3-mediated IFN-β signaling by targeting TRIF for degradation. PLoS ONE 7(10):e46825.
    • (2012) PLoS ONE , vol.7 , Issue.10
    • Xue, Q.1
  • 25
    • 0036788753 scopus 로고    scopus 로고
    • Interleukin-1 (IL-1) receptor- associated kinase-dependent IL-1-induced signaling complexes phosphorylate TAK1 and TAB2 at the plasma membrane and activate TAK1 in the cytosol
    • Jiang Z, Ninomiya-Tsuji J, Qian Y, Matsumoto K, Li X (2002) Interleukin-1 (IL-1) receptor- associated kinase-dependent IL-1-induced signaling complexes phosphorylate TAK1 and TAB2 at the plasma membrane and activate TAK1 in the cytosol. Mol Cell Biol 22(20):7158-7167.
    • (2002) Mol Cell Biol , vol.22 , Issue.20 , pp. 7158-7167
    • Jiang, Z.1    Ninomiya-Tsuji, J.2    Qian, Y.3    Matsumoto, K.4    Li, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.