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Volumn 5, Issue 1, 2013, Pages 180-193

A BRISC-SHMT Complex Deubiquitinates IFNAR1 and Regulates Interferon Responses

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; GLYCINE HYDROXYMETHYLTRANSFERASE; INTERLEUKIN 1BETA CONVERTING ENZYME; MEMBRANE PROTEIN; TYPE 1 INTERFERON RECEPTOR CHAIN; UNCLASSIFIED DRUG;

EID: 84885852890     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2013.08.025     Document Type: Article
Times cited : (82)

References (47)
  • 1
    • 75749083254 scopus 로고    scopus 로고
    • Deficiency of type I IFN receptor in lupus-prone New Zealand mixed 2328 mice decreases dendritic cell numbers and activation and protects from disease
    • Agrawal H., Jacob N., Carreras E., Bajana S., Putterman C., Turner S., Neas B., Mathian A., Koss M.N., Stohl W., et al. Deficiency of type I IFN receptor in lupus-prone New Zealand mixed 2328 mice decreases dendritic cell numbers and activation and protects from disease. J.Immunol. 2009, 183:6021-6029.
    • (2009) J.Immunol. , vol.183 , pp. 6021-6029
    • Agrawal, H.1    Jacob, N.2    Carreras, E.3    Bajana, S.4    Putterman, C.5    Turner, S.6    Neas, B.7    Mathian, A.8    Koss, M.N.9    Stohl, W.10
  • 2
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik A.Y., Hochstrasser M. Mechanism and function of deubiquitinating enzymes. Biochim. Biophys. Acta 2004, 1695:189-207.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 3
    • 0032923377 scopus 로고    scopus 로고
    • The secretory route of the leaderless protein interleukin 1beta involves exocytosis of endolysosome-related vesicles
    • Andrei C., Dazzi C., Lotti L., Torrisi M.R., Chimini G., Rubartelli A. The secretory route of the leaderless protein interleukin 1beta involves exocytosis of endolysosome-related vesicles. Mol. Biol. Cell 1999, 10:1463-1475.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1463-1475
    • Andrei, C.1    Dazzi, C.2    Lotti, L.3    Torrisi, M.R.4    Chimini, G.5    Rubartelli, A.6
  • 4
    • 9644272423 scopus 로고    scopus 로고
    • The ubiquitin system: pathogenesis of human diseases and drug targeting
    • Ciechanover A., Schwartz A.L. The ubiquitin system: pathogenesis of human diseases and drug targeting. Biochim. Biophys. Acta 2004, 1695:3-17.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 3-17
    • Ciechanover, A.1    Schwartz, A.L.2
  • 5
    • 33750302074 scopus 로고    scopus 로고
    • Endocytosis: the DUB version
    • Clague M.J., Urbé S. Endocytosis: the DUB version. Trends Cell Biol. 2006, 16:551-559.
    • (2006) Trends Cell Biol. , vol.16 , pp. 551-559
    • Clague, M.J.1    Urbé, S.2
  • 6
    • 36749082959 scopus 로고    scopus 로고
    • A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway
    • Cohn M.A., Kowal P., Yang K., Haas W., Huang T.T., Gygi S.P., D'Andrea A.D. A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway. Mol. Cell 2007, 28:786-797.
    • (2007) Mol. Cell , vol.28 , pp. 786-797
    • Cohn, M.A.1    Kowal, P.2    Yang, K.3    Haas, W.4    Huang, T.T.5    Gygi, S.P.6    D'Andrea, A.D.7
  • 7
    • 62649104153 scopus 로고    scopus 로고
    • K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1
    • Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M., Cohen R.E. K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1. EMBO J. 2009, 28:621-631.
    • (2009) EMBO J. , vol.28 , pp. 621-631
    • Cooper, E.M.1    Cutcliffe, C.2    Kristiansen, T.Z.3    Pandey, A.4    Pickart, C.M.5    Cohen, R.E.6
  • 8
    • 77951227161 scopus 로고    scopus 로고
    • Specificity of the BRISC deubiquitinating enzyme is not due to selective binding to Lys63-linked polyubiquitin
    • Cooper E.M., Boeke J.D., Cohen R.E. Specificity of the BRISC deubiquitinating enzyme is not due to selective binding to Lys63-linked polyubiquitin. J.Biol. Chem. 2010, 285:10344-10352.
    • (2010) J.Biol. Chem. , vol.285 , pp. 10344-10352
    • Cooper, E.M.1    Boeke, J.D.2    Cohen, R.E.3
  • 9
    • 77957260099 scopus 로고    scopus 로고
    • The Lys63-specific deubiquitinating enzyme BRCC36 is regulated by two scaffold proteins localizing in different subcellular compartments
    • Feng L., Wang J., Chen J. The Lys63-specific deubiquitinating enzyme BRCC36 is regulated by two scaffold proteins localizing in different subcellular compartments. J.Biol. Chem. 2010, 285:30982-30988.
    • (2010) J.Biol. Chem. , vol.285 , pp. 30982-30988
    • Feng, L.1    Wang, J.2    Chen, J.3
  • 10
    • 84861412643 scopus 로고    scopus 로고
    • Ubiquitination-mediated regulation of interferon responses
    • Fuchs S.Y. Ubiquitination-mediated regulation of interferon responses. Growth Factors 2012, 30:141-148.
    • (2012) Growth Factors , vol.30 , pp. 141-148
    • Fuchs, S.Y.1
  • 11
    • 84876100198 scopus 로고    scopus 로고
    • Hope and fear for interferon: the receptor-centric outlook on the future of interferon therapy
    • Fuchs S.Y. Hope and fear for interferon: the receptor-centric outlook on the future of interferon therapy. J.Interferon Cytokine Res. 2013, 33:211-225.
    • (2013) J.Interferon Cytokine Res. , vol.33 , pp. 211-225
    • Fuchs, S.Y.1
  • 12
    • 77950627242 scopus 로고    scopus 로고
    • IL-1 pathways in inflammation and human diseases
    • Gabay C., Lamacchia C., Palmer G. IL-1 pathways in inflammation and human diseases. Nat Rev Rheumatol 2010, 6:232-241.
    • (2010) Nat Rev Rheumatol , vol.6 , pp. 232-241
    • Gabay, C.1    Lamacchia, C.2    Palmer, G.3
  • 14
    • 84857415635 scopus 로고    scopus 로고
    • Constitutive type I interferon modulates homeostatic balance through tonic signaling
    • Gough D.J., Messina N.L., Clarke C.J., Johnstone R.W., Levy D.E. Constitutive type I interferon modulates homeostatic balance through tonic signaling. Immunity 2012, 36:166-174.
    • (2012) Immunity , vol.36 , pp. 166-174
    • Gough, D.J.1    Messina, N.L.2    Clarke, C.J.3    Johnstone, R.W.4    Levy, D.E.5
  • 15
    • 84858121800 scopus 로고    scopus 로고
    • The role of ubiquitylation in receptor endocytosis and endosomal sorting
    • Haglund K., Dikic I. The role of ubiquitylation in receptor endocytosis and endosomal sorting. J.Cell Sci. 2012, 125:265-275.
    • (2012) J.Cell Sci. , vol.125 , pp. 265-275
    • Haglund, K.1    Dikic, I.2
  • 17
    • 79251544654 scopus 로고    scopus 로고
    • Ubiquitination-dependent regulation of signaling receptors in cancer
    • Huangfu W.C., Fuchs S.Y. Ubiquitination-dependent regulation of signaling receptors in cancer. Genes Cancer 2010, 1:725-734.
    • (2010) Genes Cancer , vol.1 , pp. 725-734
    • Huangfu, W.C.1    Fuchs, S.Y.2
  • 19
    • 77953715170 scopus 로고    scopus 로고
    • Regulatory mechanisms involved in the control of ubiquitin homeostasis
    • Kimura Y., Tanaka K. Regulatory mechanisms involved in the control of ubiquitin homeostasis. J.Biochem. 2010, 147:793-798.
    • (2010) J.Biochem. , vol.147 , pp. 793-798
    • Kimura, Y.1    Tanaka, K.2
  • 20
    • 0142105396 scopus 로고    scopus 로고
    • SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation of the interferon-alpha receptor
    • Kumar K.G., Tang W., Ravindranath A.K., Clark W.A., Croze E., Fuchs S.Y. SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation of the interferon-alpha receptor. EMBO J. 2003, 22:5480-5490.
    • (2003) EMBO J. , vol.22 , pp. 5480-5490
    • Kumar, K.G.1    Tang, W.2    Ravindranath, A.K.3    Clark, W.A.4    Croze, E.5    Fuchs, S.Y.6
  • 21
    • 8744247500 scopus 로고    scopus 로고
    • Phosphorylation and specific ubiquitin acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of type I interferon receptor
    • Kumar K.G., Krolewski J.J., Fuchs S.Y. Phosphorylation and specific ubiquitin acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of type I interferon receptor. J.Biol. Chem. 2004, 279:46614-46620.
    • (2004) J.Biol. Chem. , vol.279 , pp. 46614-46620
    • Kumar, K.G.1    Krolewski, J.J.2    Fuchs, S.Y.3
  • 23
    • 49649111204 scopus 로고    scopus 로고
    • Basal ubiquitin-independent internalization of interferon alpha receptor is prevented by Tyk2-mediated masking of a linear endocytic motif
    • Kumar K.G., Varghese B., Banerjee A., Baker D.P., Constantinescu S.N., Pellegrini S., Fuchs S.Y. Basal ubiquitin-independent internalization of interferon alpha receptor is prevented by Tyk2-mediated masking of a linear endocytic motif. J.Biol. Chem. 2008, 283:18566-18572.
    • (2008) J.Biol. Chem. , vol.283 , pp. 18566-18572
    • Kumar, K.G.1    Varghese, B.2    Banerjee, A.3    Baker, D.P.4    Constantinescu, S.N.5    Pellegrini, S.6    Fuchs, S.Y.7
  • 26
    • 84868144947 scopus 로고    scopus 로고
    • Safety and pharmacodynamics of rontalizumab in patients with systemic lupus erythematosus: results of a phase I, placebo-controlled, double-blind, dose-escalation study
    • McBride J.M., Jiang J., Abbas A.R., Morimoto A., Li J., Maciuca R., Townsend M., Wallace D.J., Kennedy W.P., Drappa J. Safety and pharmacodynamics of rontalizumab in patients with systemic lupus erythematosus: results of a phase I, placebo-controlled, double-blind, dose-escalation study. Arthritis Rheum. 2012, 64:3666-3676.
    • (2012) Arthritis Rheum. , vol.64 , pp. 3666-3676
    • McBride, J.M.1    Jiang, J.2    Abbas, A.R.3    Morimoto, A.4    Li, J.5    Maciuca, R.6    Townsend, M.7    Wallace, D.J.8    Kennedy, W.P.9    Drappa, J.10
  • 29
    • 77957284673 scopus 로고    scopus 로고
    • Differential regulation of JAMM domain deubiquitinating enzyme activity within the RAP80 complex
    • Patterson-Fortin J., Shao G., Bretscher H., Messick T.E., Greenberg R.A. Differential regulation of JAMM domain deubiquitinating enzyme activity within the RAP80 complex. J.Biol. Chem. 2010, 285:30971-30981.
    • (2010) J.Biol. Chem. , vol.285 , pp. 30971-30981
    • Patterson-Fortin, J.1    Shao, G.2    Bretscher, H.3    Messick, T.E.4    Greenberg, R.A.5
  • 30
    • 84867411811 scopus 로고    scopus 로고
    • Structural and dynamic determinants of type I interferon receptor assembly and their functional interpretation
    • Piehler J., Thomas C., Garcia K.C., Schreiber G. Structural and dynamic determinants of type I interferon receptor assembly and their functional interpretation. Immunol. Rev. 2012, 250:317-334.
    • (2012) Immunol. Rev. , vol.250 , pp. 317-334
    • Piehler, J.1    Thomas, C.2    Garcia, K.C.3    Schreiber, G.4
  • 31
    • 84872782298 scopus 로고    scopus 로고
    • Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity
    • Py B.F., Kim M.S., Vakifahmetoglu-Norberg H., Yuan J. Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity. Mol. Cell 2013, 49:331-338.
    • (2013) Mol. Cell , vol.49 , pp. 331-338
    • Py, B.F.1    Kim, M.S.2    Vakifahmetoglu-Norberg, H.3    Yuan, J.4
  • 33
    • 65249186662 scopus 로고    scopus 로고
    • Polyubiquitin binding and disassembly by deubiquitinating enzymes
    • Reyes-Turcu F.E., Wilkinson K.D. Polyubiquitin binding and disassembly by deubiquitinating enzymes. Chem. Rev. 2009, 109:1495-1508.
    • (2009) Chem. Rev. , vol.109 , pp. 1495-1508
    • Reyes-Turcu, F.E.1    Wilkinson, K.D.2
  • 34
    • 13244252239 scopus 로고    scopus 로고
    • Activities of hepatic cytosolic and mitochondrial forms of serine hydroxymethyltransferase and hepatic glycine concentration are affected by vitamin B-6 intake in rats
    • Scheer J.B., Mackey A.D., Gregory J.F. Activities of hepatic cytosolic and mitochondrial forms of serine hydroxymethyltransferase and hepatic glycine concentration are affected by vitamin B-6 intake in rats. J.Nutr. 2005, 135:233-238.
    • (2005) J.Nutr. , vol.135 , pp. 233-238
    • Scheer, J.B.1    Mackey, A.D.2    Gregory, J.F.3
  • 35
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder K., Tschopp J. The inflammasomes. Cell 2010, 140:821-832.
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 36
    • 62549140202 scopus 로고    scopus 로고
    • The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks
    • Shao G., Lilli D.R., Patterson-Fortin J., Coleman K.A., Morrissey D.E., Greenberg R.A. The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks. Proc. Natl. Acad. Sci. USA 2009, 106:3166-3171.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3166-3171
    • Shao, G.1    Lilli, D.R.2    Patterson-Fortin, J.3    Coleman, K.A.4    Morrissey, D.E.5    Greenberg, R.A.6
  • 39
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa M.E., Bennett E.J., Gygi S.P., Harper J.W. Defining the human deubiquitinating enzyme interaction landscape. Cell 2009, 138:389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 40
    • 0037379578 scopus 로고    scopus 로고
    • Neutralizing interferon alpha as a therapeutic approach to autoimmune diseases
    • Stewart T.A. Neutralizing interferon alpha as a therapeutic approach to autoimmune diseases. Cytokine Growth Factor Rev. 2003, 14:139-154.
    • (2003) Cytokine Growth Factor Rev. , vol.14 , pp. 139-154
    • Stewart, T.A.1
  • 41
    • 0035344461 scopus 로고    scopus 로고
    • A weak signal for strong responses: interferon-alpha/beta revisited
    • Taniguchi T., Takaoka A. A weak signal for strong responses: interferon-alpha/beta revisited. Nat. Rev. Mol. Cell Biol. 2001, 2:378-386.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 378-386
    • Taniguchi, T.1    Takaoka, A.2
  • 42
    • 77957745555 scopus 로고    scopus 로고
    • Type I interferon: friend or foe?
    • Trinchieri G. Type I interferon: friend or foe?. J.Exp. Med. 2010, 207:2053-2063.
    • (2010) J.Exp. Med. , vol.207 , pp. 2053-2063
    • Trinchieri, G.1
  • 43
    • 50949126350 scopus 로고    scopus 로고
    • Protein partners of deubiquitinating enzymes
    • Ventii K.H., Wilkinson K.D. Protein partners of deubiquitinating enzymes. Biochem. J. 2008, 414:161-175.
    • (2008) Biochem. J. , vol.414 , pp. 161-175
    • Ventii, K.H.1    Wilkinson, K.D.2
  • 45
    • 0033603199 scopus 로고    scopus 로고
    • Dynamic regulation of the proinflammatory cytokine, interleukin-1beta: molecular biology for non-molecular biologists
    • Watkins L.R., Hansen M.K., Nguyen K.T., Lee J.E., Maier S.F. Dynamic regulation of the proinflammatory cytokine, interleukin-1beta: molecular biology for non-molecular biologists. Life Sci. 1999, 65:449-481.
    • (1999) Life Sci. , vol.65 , pp. 449-481
    • Watkins, L.R.1    Hansen, M.K.2    Nguyen, K.T.3    Lee, J.E.4    Maier, S.F.5
  • 46
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao T., Cohen R.E. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 2002, 419:403-407.
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 47
    • 79251574143 scopus 로고    scopus 로고
    • Ligand-stimulated downregulation of the alpha interferon receptor: role of protein kinase D2
    • Zheng H., Qian J., Varghese B., Baker D.P., Fuchs S. Ligand-stimulated downregulation of the alpha interferon receptor: role of protein kinase D2. Mol. Cell. Biol. 2011, 31:710-720.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 710-720
    • Zheng, H.1    Qian, J.2    Varghese, B.3    Baker, D.P.4    Fuchs, S.5


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