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Volumn 12, Issue 8, 2013, Pages 2136-2147

Multi-omic data integration links deleted in breast cancer 1 (DBC1) degradation to chromatin remodeling in inflammatory response

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; LIPOPOLYSACCHARIDE; PROTEIN DBC1; UNCLASSIFIED DRUG; CHROMATIN; DBC1 PROTEIN, HUMAN; PROTEOME; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TRANSCRIPTOME; TUMOR SUPPRESSOR PROTEIN; UBIQUITINATED PROTEIN;

EID: 84881111008     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.026138     Document Type: Article
Times cited : (2)

References (53)
  • 1
    • 79955620198 scopus 로고    scopus 로고
    • Constructing and decoding unconventional ubiquitin chains
    • Behrends, C., and Harper, J. W. (2011) Constructing and decoding unconventional ubiquitin chains. Nat. Struct. Mol. Biol. 18, 520-528
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 520-528
    • Behrends, C.1    Harper, J.W.2
  • 2
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • Reyes-Turcu, F. E., VentIII, K. H., and Wilkinson, K. D. (2009) Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu. Rev. Biochem. 78, 363-397
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1    Ventii, K.H.2    Wilkinson, K.D.3
  • 3
    • 84655176306 scopus 로고    scopus 로고
    • The role of ubiquitylation in immune defence and pathogen evasion
    • Jiang, X., and Chen, Z. J. (2011) The role of ubiquitylation in immune defence and pathogen evasion. Nat. Rev. Immunol. 12, 35-48
    • (2011) Nat. Rev. Immunol. , vol.12 , pp. 35-48
    • Jiang, X.1    Chen, Z.J.2
  • 4
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: Update on Toll-like receptors
    • Kawai, T., and Akira, S. (2010) The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat. Immunol. 11, 373-384
    • (2010) Nat. Immunol. , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 5
    • 75249101443 scopus 로고    scopus 로고
    • Hijacking the host ubiquitin pathway: Structural strategies of bacterial E3 ubiquitin ligases
    • Hicks, S. W., and Galan, J. E. (2010) Hijacking the host ubiquitin pathway: structural strategies of bacterial E3 ubiquitin ligases. Curr. Opin. Microbiol. 13, 41-46
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 41-46
    • Hicks, S.W.1    Galan, J.E.2
  • 8
    • 34250782684 scopus 로고    scopus 로고
    • Extraction, purification and analysis of histones
    • Shechter, D., Dormann, H. L., Allis, C. D., and Hake, S. B. (2007) Extraction, purification and analysis of histones. Nat. Protoc. 2, 1445-1457
    • (2007) Nat. Protoc. , vol.2 , pp. 1445-1457
    • Shechter, D.1    Dormann, H.L.2    Allis, C.D.3    Hake, S.B.4
  • 9
    • 0037154160 scopus 로고    scopus 로고
    • Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
    • Funakoshi, M., Sasaki, T., Nishimoto, T., and Kobayashi, H. (2002) Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc. Natl. Acad. Sci. U.S.A. 99, 745-750
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 745-750
    • Funakoshi, M.1    Sasaki, T.2    Nishimoto, T.3    Kobayashi, H.4
  • 13
    • 50149117169 scopus 로고    scopus 로고
    • Spectral probabilities and generating functions of tandem mass spectra: A strike against decoy databases
    • Kim, S., Gupta, N., and Pevzner, P. A. (2008) Spectral probabilities and generating functions of tandem mass spectra: a strike against decoy databases. J. Proteome Res. 7, 3354-3363
    • (2008) J. Proteome Res. , vol.7 , pp. 3354-3363
    • Kim, S.1    Gupta, N.2    Pevzner, P.A.3
  • 15
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da, W., Sherman, B. T., and Lempicki, R. A. (2009) Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 4, 44-57
    • (2009) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang Da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 17
    • 84861234337 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetase-interacting multifunctional protein-1 (AIMP1): The member of a molecular hub with unexpected functions, including CD4 T cell homeostasis
    • Burastero, S. E., and Fabbri, M. (2012) Aminoacyl-tRNA synthetase-interacting multifunctional protein-1 (AIMP1): the member of a molecular hub with unexpected functions, including CD4 T cell homeostasis. Clin. Immunol. 143, 207-209
    • (2012) Clin. Immunol. , vol.143 , pp. 207-209
    • Burastero, S.E.1    Fabbri, M.2
  • 18
    • 38049083888 scopus 로고    scopus 로고
    • Primer: Inflammasomes and interleukin 1beta in inflammatory disorders
    • Church, L. D., Cook, G. P., and McDermott, M. F. (2008) Primer: inflammasomes and interleukin 1beta in inflammatory disorders. Nat. Clin. Pract. Rheumatol. 4, 34-42
    • (2008) Nat. Clin. Pract. Rheumatol. , vol.4 , pp. 34-42
    • Church, L.D.1    Cook, G.P.2    McDermott, M.F.3
  • 19
    • 77953377110 scopus 로고    scopus 로고
    • Hemoglobin transforms anti-inflammatory Salmonella typhi virulence polysaccharide into a TLR-2 agonist
    • Garg, R., and Qadri, A. (2010) Hemoglobin transforms anti-inflammatory Salmonella typhi virulence polysaccharide into a TLR-2 agonist. J. Immunol. 184, 5980-5987
    • (2010) J. Immunol. , vol.184 , pp. 5980-5987
    • Garg, R.1    Qadri, A.2
  • 20
    • 57749107726 scopus 로고    scopus 로고
    • FLN29 deficiency reveals its negative regulatory role in the Toll-like receptor (TLR) and retinoic acid-inducible gene i (RIG-I)-like helicase signaling pathway
    • Sanada, T., Takaesu, G., Mashima, R., Yoshida, R., Kobayashi, T., and Yoshimura, A. (2008) FLN29 deficiency reveals its negative regulatory role in the Toll-like receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like helicase signaling pathway. J. Biol. Chem. 283, 33858-33864
    • (2008) J. Biol. Chem. , vol.283 , pp. 33858-33864
    • Sanada, T.1    Takaesu, G.2    Mashima, R.3    Yoshida, R.4    Kobayashi, T.5    Yoshimura, A.6
  • 22
    • 70450252183 scopus 로고    scopus 로고
    • RIOK3 interacts with caspase-10 and negatively regulates the NF-kappaB signaling pathway
    • Shan, J., Wang, P., Zhou, J., Wu, D., Shi, H., and Huo, K. (2009) RIOK3 interacts with caspase-10 and negatively regulates the NF-kappaB signaling pathway. Mol. Cell. Biochem. 332, 113-120
    • (2009) Mol. Cell. Biochem. , vol.332 , pp. 113-120
    • Shan, J.1    Wang, P.2    Zhou, J.3    Wu, D.4    Shi, H.5    Huo, K.6
  • 24
    • 78651402182 scopus 로고    scopus 로고
    • A CSF-1 receptor phosphotyrosine 559 signaling pathway regulates receptor ubiquitination and tyrosine phosphorylation
    • Xiong, Y., Song, D., Cai, Y., Yu, W., Yeung, Y. G., and Stanley, E. R. (2011) A CSF-1 receptor phosphotyrosine 559 signaling pathway regulates receptor ubiquitination and tyrosine phosphorylation. J. Biol. Chem. 286, 952-960
    • (2011) J. Biol. Chem. , vol.286 , pp. 952-960
    • Xiong, Y.1    Song, D.2    Cai, Y.3    Yu, W.4    Yeung, Y.G.5    Stanley, E.R.6
  • 25
    • 60549100850 scopus 로고    scopus 로고
    • Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3
    • Todi, S. V., Winborn, B. J., Scaglione, K. M., Blount, J. R., Travis, S. M., and Paulson, H. L. (2009) Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3. EMBO J. 28, 372-382
    • (2009) EMBO J. , vol.28 , pp. 372-382
    • Todi, S.V.1    Winborn, B.J.2    Scaglione, K.M.3    Blount, J.R.4    Travis, S.M.5    Paulson, H.L.6
  • 26
    • 0042847104 scopus 로고    scopus 로고
    • The proteasome as a lipopolysaccharide- binding protein in macrophages: Differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events
    • Qureshi, N., Perera, P. Y., Shen, J., Zhang, G., Lenschat, A., Splitter, G., Morrison, D. C., and Vogel, S. N. (2003) The proteasome as a lipopolysaccharide- binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events. J. Immunol. 171, 1515-1525
    • (2003) J. Immunol. , vol.171 , pp. 1515-1525
    • Qureshi, N.1    Perera, P.Y.2    Shen, J.3    Zhang, G.4    Lenschat, A.5    Splitter, G.6    Morrison, D.C.7    Vogel, S.N.8
  • 28
    • 0036968725 scopus 로고    scopus 로고
    • Proteasome-dependent processing of nuclear proteins is correlated with their subnuclear localization
    • Dino Rockel, T., and von Mikecz, A. (2002) Proteasome-dependent processing of nuclear proteins is correlated with their subnuclear localization. J. Struct. Biol. 140, 189-199
    • (2002) J. Struct. Biol. , vol.140 , pp. 189-199
    • Dino Rockel, T.1    Von Mikecz, A.2
  • 29
    • 43049138051 scopus 로고    scopus 로고
    • Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
    • Kraft, C., Deplazes, A., Sohrmann, M., and Peter, M. (2008) Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat. Cell. Biol. 10, 602-610
    • (2008) Nat. Cell. Biol. , vol.10 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 31
    • 78651065175 scopus 로고    scopus 로고
    • The ubiquitin C-terminal hydrolase UCH-L1 promotes bacterial invasion by altering the dynamics of the actin cytoskeleton
    • Basseres, E., Coppotelli, G., Pfirrmann, T., Andersen, J. B., Masucci, M., and Frisan, T. (2010) The ubiquitin C-terminal hydrolase UCH-L1 promotes bacterial invasion by altering the dynamics of the actin cytoskeleton. Cell. Microbiol. 12, 1622-1633
    • (2010) Cell. Microbiol. , vol.12 , pp. 1622-1633
    • Basseres, E.1    Coppotelli, G.2    Pfirrmann, T.3    Andersen, J.B.4    Masucci, M.5    Frisan, T.6
  • 32
    • 78650411683 scopus 로고    scopus 로고
    • HDAC3 is negatively regulated by the nuclear protein DBC1
    • Chini, C. C., Escande, C., Nin, V., and Chini, E. N. (2010) HDAC3 is negatively regulated by the nuclear protein DBC1. J. Biol. Chem. 285, 40830-40837
    • (2010) J. Biol. Chem. , vol.285 , pp. 40830-40837
    • Chini, C.C.1    Escande, C.2    Nin, V.3    Chini, E.N.4
  • 33
    • 23744485726 scopus 로고    scopus 로고
    • Caspasedependent processing activates the proapoptotic activity of deleted in breast cancer-1 during tumor necrosis factor-Alpha-mediated death signaling
    • Sundararajan, R., Chen, G., Mukherjee, C., and White, E. (2005) Caspasedependent processing activates the proapoptotic activity of deleted in breast cancer-1 during tumor necrosis factor-Alpha-mediated death signaling. Oncogene 24, 4908-4920
    • (2005) Oncogene , vol.24 , pp. 4908-4920
    • Sundararajan, R.1    Chen, G.2    Mukherjee, C.3    White, E.4
  • 34
    • 38749132992 scopus 로고    scopus 로고
    • Negative regulation of the deacetylase SIRT1 by DBC1
    • Zhao, W., Kruse, J. P., Tang, Y., Jung, S. Y., Qin, J., and Gu, W. (2008) Negative regulation of the deacetylase SIRT1 by DBC1. Nature 451, 587-590
    • (2008) Nature , vol.451 , pp. 587-590
    • Zhao, W.1    Kruse, J.P.2    Tang, Y.3    Jung, S.Y.4    Qin, J.5    Gu, W.6
  • 37
    • 0035119296 scopus 로고    scopus 로고
    • Inhibition of caspase 3 abrogates lipopolysaccharide- induced nitric oxide production by preventing activation of NF-kappaB and c-Jun NH2-terminal kinase/stress-Activated protein kinase in RAW 27 murine macrophage cells
    • Chakravortty, D., Kato, Y., Sugiyama, T., Koide, N., Mu, M. M., Yoshida, T., and Yokochi, T. (2001) Inhibition of caspase 3 abrogates lipopolysaccharide- induced nitric oxide production by preventing activation of NF-kappaB and c-Jun NH2-terminal kinase/stress-Activated protein kinase in RAW 27 murine macrophage cells. Infect. Immun. 69, 1315-1321
    • (2001) Infect. Immun. , vol.69 , pp. 1315-1321
    • Chakravortty, D.1    Kato, Y.2    Sugiyama, T.3    Koide, N.4    Mu, M.M.5    Yoshida, T.6    Yokochi, T.7
  • 38
    • 0035902601 scopus 로고    scopus 로고
    • Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-Apoptotic effect in Fas-induced cell death
    • Suzuki, Y., Nakabayashi, Y., and Takahashi, R. (2001) Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-Apoptotic effect in Fas-induced cell death. Proc. Natl. Acad. Sci. U.S.A. 98, 8662-8667
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8662-8667
    • Suzuki, Y.1    Nakabayashi, Y.2    Takahashi, R.3
  • 39
    • 34250823515 scopus 로고    scopus 로고
    • Gene-specific control of inflammation by TLR-induced chromatin modifications
    • Foster, S. L., Hargreaves, D. C., and Medzhitov, R. (2007) Gene-specific control of inflammation by TLR-induced chromatin modifications. Nature 447, 972-978
    • (2007) Nature , vol.447 , pp. 972-978
    • Foster, S.L.1    Hargreaves, D.C.2    Medzhitov, R.3
  • 40
    • 59149085480 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of macrophage rafts reveals compartmentalized activation of the proteasome and of proteasome-mediated ERK activation in response to lipopolysaccharide
    • Dhungana, S., Merrick, B. A., Tomer, K. B., and Fessler, M. B. (2009) Quantitative proteomics analysis of macrophage rafts reveals compartmentalized activation of the proteasome and of proteasome-mediated ERK activation in response to lipopolysaccharide. Mol. Cell. Proteomics 8, 201-213
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 201-213
    • Dhungana, S.1    Merrick, B.A.2    Tomer, K.B.3    Fessler, M.B.4
  • 41
    • 84858725584 scopus 로고    scopus 로고
    • Regulation of NF-kappaB by deubiquitinases
    • Harhaj, E. W., and Dixit, V. M. (2012) Regulation of NF-kappaB by deubiquitinases. Immunol. Rev. 246, 107-124
    • (2012) Immunol. Rev. , vol.246 , pp. 107-124
    • Harhaj, E.W.1    Dixit, V.M.2
  • 42
    • 84859507872 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 4 mitigates Toll-like/interleukin-1 receptor signaling and regulates innate immune activation
    • Zhou, F., Zhang, X., Dam, H. V., Dijke, P. T., Huang, H., and Zhang, L. (2012) Ubiquitin-specific protease 4 mitigates Toll-like/interleukin-1 receptor signaling and regulates innate immune activation. J. Biol. Chem. 287, 11002-11010
    • (2012) J. Biol. Chem. , vol.287 , pp. 11002-11010
    • Zhou, F.1    Zhang, X.2    Dam, H.V.3    Dijke, P.T.4    Huang, H.5    Zhang, L.6
  • 43
    • 18144368948 scopus 로고    scopus 로고
    • Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase gamma-dependent phosphorylation
    • Reiley, W., Zhang, M., Wu, X., Granger, E., and Sun, S. C. (2005) Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase gamma-dependent phosphorylation. Mol. Cell. Biol. 25, 3886-3895
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3886-3895
    • Reiley, W.1    Zhang, M.2    Wu, X.3    Granger, E.4    Sun, S.C.5
  • 44
    • 0034672626 scopus 로고    scopus 로고
    • Lipopolysaccharide induces the expression of cellular inhibitor of apoptosis protein-2 in human macrophages
    • Cui, X., Imaizumi, T., Yoshida, H., Tanji, K., Matsumiya, T., and Satoh, K. (2000) Lipopolysaccharide induces the expression of cellular inhibitor of apoptosis protein-2 in human macrophages. Biochim. Biophys. Acta 1524, 178-182
    • (2000) Biochim. Biophys. Acta , vol.1524 , pp. 178-182
    • Cui, X.1    Imaizumi, T.2    Yoshida, H.3    Tanji, K.4    Matsumiya, T.5    Satoh, K.6
  • 49
    • 0037497184 scopus 로고    scopus 로고
    • A nucleosomal function for IkappaB kinasealpha in NF-kappaB-dependent gene expression
    • Anest, V., Hanson, J. L., Cogswell, P. C., Steinbrecher, K. A., Strahl, B. D., and Baldwin, A. S. (2003) A nucleosomal function for IkappaB kinasealpha in NF-kappaB-dependent gene expression. Nature 423, 659-663
    • (2003) Nature , vol.423 , pp. 659-663
    • Anest, V.1    Hanson, J.L.2    Cogswell, P.C.3    Steinbrecher, K.A.4    Strahl, B.D.5    Baldwin, A.S.6
  • 50
    • 34548644772 scopus 로고    scopus 로고
    • The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing
    • De Santa, F., Totaro, M. G., Prosperini, E., Notarbartolo, S., Testa, G., and Natoli, G. (2007) The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing. Cell 130, 1083-1094
    • (2007) Cell , vol.130 , pp. 1083-1094
    • De Santa, F.1    Totaro, M.G.2    Prosperini, E.3    Notarbartolo, S.4    Testa, G.5    Natoli, G.6
  • 51
    • 0038511129 scopus 로고    scopus 로고
    • Histone H3 phosphorylation by IKK-Alpha is critical for cytokineinduced gene expression
    • Yamamoto, Y., Verma, U. N., Prajapati, S., Kwak, Y. T., and Gaynor, R. B. (2003) Histone H3 phosphorylation by IKK-Alpha is critical for cytokineinduced gene expression. Nature 423, 655-659
    • (2003) Nature , vol.423 , pp. 655-659
    • Yamamoto, Y.1    Verma, U.N.2    Prajapati, S.3    Kwak, Y.T.4    Gaynor, R.B.5
  • 52
    • 38149098408 scopus 로고    scopus 로고
    • Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase III transcriptional elongation
    • Zhou, W., Zhu, P., Wang, J., Pascual, G., Ohgi, K. A., Lozach, J., Glass, C. K., and Rosenfeld, M. G. (2008) Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase III transcriptional elongation. Mol. Cell 29, 69-80
    • (2008) Mol. Cell , vol.29 , pp. 69-80
    • Zhou, W.1    Zhu, P.2    Wang, J.3    Pascual, G.4    Ohgi, K.A.5    Lozach, J.6    Glass, C.K.7    Rosenfeld, M.G.8
  • 53
    • 70349443224 scopus 로고    scopus 로고
    • Transcriptional control of the inflammatory response
    • Medzhitov, R., and Horng, T. (2009) Transcriptional control of the inflammatory response. Nat. Rev. Immunol. 9, 692-703
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 692-703
    • Medzhitov, R.1    Horng, T.2


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