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Volumn 27, Issue 25, 2008, Pages 3516-3526

Copine-I represses NF-κB transcription by endoproteolysis of p65

Author keywords

Copine I; Endoproteolysis; NF B; p65; Repressor; Transcription

Indexed keywords

COPINE I; I KAPPA B ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; P65 PROTEIN; PHOSPHOLIPID BINDING PROTEIN; PROTEIN DERIVATIVE; SMALL INTERFERING RNA; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR ALPHA;

EID: 44849111192     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/sj.onc.1211030     Document Type: Article
Times cited : (40)

References (42)
  • 1
    • 0034802887 scopus 로고    scopus 로고
    • The p65 (RelA) subunit of NF-κB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression
    • Ashburner BP, Westerheide SD, Baldwin Jr AS. (2001). The p65 (RelA) subunit of NF-κB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression. Mol Cell Biol 21: 7065-7077.
    • (2001) Mol Cell Biol , vol.21 , pp. 7065-7077
    • Ashburner, B.P.1    Westerheide, S.D.2    Baldwin Jr, A.S.3
  • 2
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and IκBproteins: New discoveries and insights
    • Baldwin AS. (1996). The NF-κB and IκBproteins: new discoveries and insights. Annu Rev Immunol 14: 649-681.
    • (1996) Annu Rev Immunol , vol.14 , pp. 649-681
    • Baldwin, A.S.1
  • 4
    • 0032556894 scopus 로고    scopus 로고
    • Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA
    • Chen FE, Huang DB, Chen YQ, Ghosh G. (1998). Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA. Nature 391: 410-413.
    • (1998) Nature , vol.391 , pp. 410-413
    • Chen, F.E.1    Huang, D.B.2    Chen, Y.Q.3    Ghosh, G.4
  • 5
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-kappa B action regulated by reversible acetylation
    • Chen LF, Fischle W, Verdin E, Greene WC. (2001). Duration of nuclear NF-kappa B action regulated by reversible acetylation. Science 293: 1653-1657.
    • (2001) Science , vol.293 , pp. 1653-1657
    • Chen, L.F.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 7
    • 0031964687 scopus 로고    scopus 로고
    • A novel DNA recognition mode by the NF-kappa B p65 homodimer
    • Chen YQ, Ghosh S, Ghosh G. (1998). A novel DNA recognition mode by the NF-kappa B p65 homodimer. Nat Struct Biol 5: 67-73.
    • (1998) Nat Struct Biol , vol.5 , pp. 67-73
    • Chen, Y.Q.1    Ghosh, S.2    Ghosh, G.3
  • 8
    • 0031939689 scopus 로고    scopus 로고
    • The copines, a novel class of C2 domain-containing, calcium-dependent, phospholipid-binding proteins conserved from Paramecium to humans
    • Creutz CE, Tomsig JL, Snyder SL, Gautier MC, Skouri F, Beisson J et al. (1998). The copines, a novel class of C2 domain-containing, calcium-dependent, phospholipid-binding proteins conserved from Paramecium to humans. J Biol Chem 273: 1393-1402.
    • (1998) J Biol Chem , vol.273 , pp. 1393-1402
    • Creutz, C.E.1    Tomsig, J.L.2    Snyder, S.L.3    Gautier, M.C.4    Skouri, F.5    Beisson, J.6
  • 9
    • 0347361648 scopus 로고    scopus 로고
    • Interaction of proteinase 3 with CD11b/CD18( b2integrin) on the cell membrane of human neutrophils
    • David A, Kacher Y, Specks U, Aviram I. (2003). Interaction of proteinase 3 with CD11b/CD18( b2integrin) on the cell membrane of human neutrophils. J Leukoc Biol 74: 551-557.
    • (2003) J Leukoc Biol , vol.74 , pp. 551-557
    • David, A.1    Kacher, Y.2    Specks, U.3    Aviram, I.4
  • 10
    • 0031866394 scopus 로고    scopus 로고
    • Ligand recognition by the I domain-containing integrins
    • Dickeson SK, Santoro SA. (1998). Ligand recognition by the I domain-containing integrins. Cell Mol Life Sci 54: 556-566.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 556-566
    • Dickeson, S.K.1    Santoro, S.A.2
  • 11
    • 0035885972 scopus 로고    scopus 로고
    • Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family
    • Fujikawa K, Suzuki H, McMullen B, Chung D. (2001). Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family. Blood 98: 1662-1666.
    • (2001) Blood , vol.98 , pp. 1662-1666
    • Fujikawa, K.1    Suzuki, H.2    McMullen, B.3    Chung, D.4
  • 12
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-κB
    • Hayden MS, Ghosh S. (2004). Signaling to NF-κB. Genes Dev 18: 2195-2224.
    • (2004) Genes Dev , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 13
    • 30744458869 scopus 로고    scopus 로고
    • IκB kinase α-mediated derepression of SMRT potentiates acetylation of RelA/p65 by p300
    • Hoberg JE, Popko AE, Ramsey CS, Mayo MW. (2006). IκB kinase α-mediated derepression of SMRT potentiates acetylation of RelA/p65 by p300. Mol Cell Biol 26: 457-471.
    • (2006) Mol Cell Biol , vol.26 , pp. 457-471
    • Hoberg, J.E.1    Popko, A.E.2    Ramsey, C.S.3    Mayo, M.W.4
  • 14
    • 6344241039 scopus 로고    scopus 로고
    • SMRT derepression by the IκB kinase α: A prerequisite to NF-κB transcription and survival
    • Hoberg JE, Yeung F, Mayo MW. (2004). SMRT derepression by the IκB kinase α: a prerequisite to NF-κB transcription and survival. Mol Cell 16: 245-255.
    • (2004) Mol Cell , vol.16 , pp. 245-255
    • Hoberg, J.E.1    Yeung, F.2    Mayo, M.W.3
  • 16
    • 4344612243 scopus 로고    scopus 로고
    • NF-κB is essential for epithelialmesenchymal transition and metastasis in a model of breast cancer progression
    • Huber MA, Azoitei N, Baumann B, Grunert S, Sommer A, Pehamberger H et al. (2004). NF-κB is essential for epithelialmesenchymal transition and metastasis in a model of breast cancer progression. J Clin Invest 114: 569-581.
    • (2004) J Clin Invest , vol.114 , pp. 569-581
    • Huber, M.A.1    Azoitei, N.2    Baumann, B.3    Grunert, S.4    Sommer, A.5    Pehamberger, H.6
  • 17
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IκBá/NF- κB Complex
    • Jacobs MD, Harrison SC. (1998). Structure of an IκBá/NF- κB Complex. Cell 95: 749-758.
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 18
    • 0035816561 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of the NF-κB subunit p65 at the NH2 terminus potentiates naphthoquinone analog-induced apoptosis
    • Kang KH, Lee KH, Kim MY, Choi KH. (2001). Caspase-3-mediated cleavage of the NF-κB subunit p65 at the NH2 terminus potentiates naphthoquinone analog-induced apoptosis. J Biol Chem 276: 24638-24644.
    • (2001) J Biol Chem , vol.276 , pp. 24638-24644
    • Kang, K.H.1    Lee, K.H.2    Kim, M.Y.3    Choi, K.H.4
  • 19
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-κB activity
    • Karin M, Ben Neriah Y. (2000). Phosphorylation meets ubiquitination: the control of NF-κB activity. Annu Rev Immunol 18: 621-663.
    • (2000) Annu Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben Neriah, Y.2
  • 20
    • 25844459154 scopus 로고    scopus 로고
    • NF-κB: Linking inflammation and immunity to cancer development and progression
    • Karin M, Greten FR. (2005). NF-κB: linking inflammation and immunity to cancer development and progression. Nat Rev Immunol 5: 749-759.
    • (2005) Nat Rev Immunol , vol.5 , pp. 749-759
    • Karin, M.1    Greten, F.R.2
  • 21
    • 19944427622 scopus 로고    scopus 로고
    • Determination of genes relative to gastrointestinal tract origin cancers cells using a cDNA microarray
    • Kim TM, Jeong HJ, Seo MY, Kim SC, Park KH, Park CH et al. (2005). Determination of genes relative to gastrointestinal tract origin cancers cells using a cDNA microarray. Clin Cancer Res 11: 79-86.
    • (2005) Clin Cancer Res , vol.11 , pp. 79-86
    • Kim, T.M.1    Jeong, H.J.2    Seo, M.Y.3    Kim, S.C.4    Park, K.H.5    Park, C.H.6
  • 22
    • 0034668005 scopus 로고    scopus 로고
    • The soluble endothelial protein C receptor binds to activated neutrophils: Involvement of proteinase-3 and CD11b/CD18
    • Kurosawa S, Esmon CT, Stearns-Kurosawa DJ. (2000). The soluble endothelial protein C receptor binds to activated neutrophils: involvement of proteinase-3 and CD11b/CD18. J Immunol 165: 4697-4703.
    • (2000) J Immunol , vol.165 , pp. 4697-4703
    • Kurosawa, S.1    Esmon, C.T.2    Stearns-Kurosawa, D.J.3
  • 23
    • 0033174072 scopus 로고    scopus 로고
    • Apoptosis overrides survival signals through a caspase-mediated dominant-negative NF-κB loop
    • Levkau B, Scatena M, Giachelli CM, Ross R, Raines EW. (1999). Apoptosis overrides survival signals through a caspase-mediated dominant-negative NF-κB loop. Nat Cell Biol 1: 227-233.
    • (1999) Nat Cell Biol , vol.1 , pp. 227-233
    • Levkau, B.1    Scatena, M.2    Giachelli, C.M.3    Ross, R.4    Raines, E.W.5
  • 24
    • 9144264169 scopus 로고    scopus 로고
    • A map of the interactome network of the metazoan C. elegans
    • Li S, Armstrong CM, Bertin N, Ge H, Milstein S, Boxem M et al. (2004). A map of the interactome network of the metazoan C. elegans. Science 303: 540-543.
    • (2004) Science , vol.303 , pp. 540-543
    • Li, S.1    Armstrong, C.M.2    Bertin, N.3    Ge, H.4    Milstein, S.5    Boxem, M.6
  • 25
    • 0029924035 scopus 로고    scopus 로고
    • A glycine-rich region in NF-kappaB p105 functions as a processing signal for the generation of the p50 subunit
    • Lin L, Ghosh S. (1996). A glycine-rich region in NF-kappaB p105 functions as a processing signal for the generation of the p50 subunit. Mol Cell Biol 16: 2248-2254.
    • (1996) Mol Cell Biol , vol.16 , pp. 2248-2254
    • Lin, L.1    Ghosh, S.2
  • 26
    • 33846475712 scopus 로고    scopus 로고
    • COMMD1 promotes the ubiquitination of NF-κB subunits through a cullin-containing ubiquitin ligase
    • Maine GN, Mao X, Komarck CM, Burstein E. (2007). COMMD1 promotes the ubiquitination of NF-κB subunits through a cullin-containing ubiquitin ligase. EMBO J 26: 436-447.
    • (2007) EMBO J , vol.26 , pp. 436-447
    • Maine, G.N.1    Mao, X.2    Komarck, C.M.3    Burstein, E.4
  • 28
    • 0037192829 scopus 로고    scopus 로고
    • PTEN blocks TNF-induced NF-κB-dependent transcription by inhibiting the transactivation potential of p65 subunit
    • Mayo MW, Madrid LV, Westerheide SD, Jones DR, Yuan X-J, Baldwin AS et al. (2002). PTEN blocks TNF-induced NF-κB-dependent transcription by inhibiting the transactivation potential of p65 subunit. J Biol Chem 277: 11116-11125.
    • (2002) J Biol Chem , vol.277 , pp. 11116-11125
    • Mayo, M.W.1    Madrid, L.V.2    Westerheide, S.D.3    Jones, D.R.4    Yuan, X.-J.5    Baldwin, A.S.6
  • 29
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • Nalefski EA, Falke JJ. (1996). The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci 5: 2375-2390.
    • (1996) Protein Sci , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 30
  • 31
    • 0036892507 scopus 로고    scopus 로고
    • Novel effects of neutrophil-derived proteinase 3 and elastase on the vascular endothelium involve in vivo cleavage of NF-κB and proapoptotic changes in JNK, ERK, and p38M APK signaling pathways
    • Preston GA, Zarella CS, Pendergraft III WF, Rudolph EH, Yang JJ, Sekura SB et al. (2002). Novel effects of neutrophil-derived proteinase 3 and elastase on the vascular endothelium involve in vivo cleavage of NF-κB and proapoptotic changes in JNK, ERK, and p38M APK signaling pathways. J Am Soc Nephrol 13: 2840-2849.
    • (2002) J Am Soc Nephrol , vol.13 , pp. 2840-2849
    • Preston, G.A.1    Zarella, C.S.2    Pendergraft III, W.F.3    Rudolph, E.H.4    Yang, J.J.5    Sekura, S.B.6
  • 33
    • 0026570254 scopus 로고
    • Functional characterization of the NF-kappa B p65 transcriptional activator and an alternatively spliced derivative
    • Ruben SM, Narayanan R, Klement JF, Chen CH, Rosen CA. (1992). Functional characterization of the NF-kappa B p65 transcriptional activator and an alternatively spliced derivative. Mol Cell Biol 12: 444-454.
    • (1992) Mol Cell Biol , vol.12 , pp. 444-454
    • Ruben, S.M.1    Narayanan, R.2    Klement, J.F.3    Chen, C.H.4    Rosen, C.A.5
  • 34
    • 3142771914 scopus 로고    scopus 로고
    • Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor κB response
    • Saccani S, Marazzi I, Beg AA, Natoli G. (2004). Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor κB response. J Exp Med 200: 107-113.
    • (2004) J Exp Med , vol.200 , pp. 107-113
    • Saccani, S.1    Marazzi, I.2    Beg, A.A.3    Natoli, G.4
  • 35
    • 0034719141 scopus 로고    scopus 로고
    • 2+-dependent, phospholipid-binding protein
    • 2+-dependent, phospholipid-binding protein. Biochemistry 39: 16163-16175.
    • (2000) Biochemistry , vol.39 , pp. 16163-16175
    • Tomsig, J.L.1    Creutz, C.E.2
  • 37
    • 0038532315 scopus 로고    scopus 로고
    • Identification of targets for calcium signaling through the copine family of proteins - characterization of a coiled-coil copine-binding motif
    • Tomsig JL, Snyder SL, Creutz CE. (2003). Identification of targets for calcium signaling through the copine family of proteins - characterization of a coiled-coil copine-binding motif. J Biol Chem 278: 10048-10054.
    • (2003) J Biol Chem , vol.278 , pp. 10048-10054
    • Tomsig, J.L.1    Snyder, S.L.2    Creutz, C.E.3
  • 38
    • 1642504844 scopus 로고    scopus 로고
    • Calcium-dependent regulation of tumour necrosis factor-α receptor signalling by copine
    • Tomsig JL, Sohma H, Creutz CE. (2004). Calcium-dependent regulation of tumour necrosis factor-α receptor signalling by copine. Biochem J 378: 1089-1094.
    • (2004) Biochem J , vol.378 , pp. 1089-1094
    • Tomsig, J.L.1    Sohma, H.2    Creutz, C.E.3
  • 39
    • 0036796740 scopus 로고    scopus 로고
    • Distribution and evolution of von Willebrand/integrin A domains: Widely dispersed domains with roles in cell adhesion and elsewhere
    • Whittaker CA, Hynes RO. (2002). Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere. Mol Biol Cell 13: 3369-3387.
    • (2002) Mol Biol Cell , vol.13 , pp. 3369-3387
    • Whittaker, C.A.1    Hynes, R.O.2
  • 40
    • 0036792564 scopus 로고    scopus 로고
    • Differential gene expression patterns in HER2/neu- positive and -negative breast cancer cell lines and tissues
    • Wilson KS, Roberts H, Leek R, Harris AL, Geradts J. (2002). Differential gene expression patterns in HER2/neu- positive and -negative breast cancer cell lines and tissues. Am J Pathol 161: 1171-1185.
    • (2002) Am J Pathol , vol.161 , pp. 1171-1185
    • Wilson, K.S.1    Roberts, H.2    Leek, R.3    Harris, A.L.4    Geradts, J.5
  • 41
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F, Hoberg JE, Ramsey CS, Keller MD, Jones DR, Frye R et al. (2004). Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J 23: 2369-2380.
    • (2004) EMBO J , vol.23 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3    Keller, M.D.4    Jones, D.R.5    Frye, R.6
  • 42
    • 0036203419 scopus 로고    scopus 로고
    • The phosphorylation status of nuclear NF-κB determines its association with CBP/p300 or HDAC1
    • Zhong HH, May MJ, Jimi E, Ghosh S. (2002). The phosphorylation status of nuclear NF-κB determines its association with CBP/p300 or HDAC1. Mol Cell 9: 625-636.
    • (2002) Mol Cell , vol.9 , pp. 625-636
    • Zhong, H.H.1    May, M.J.2    Jimi, E.3    Ghosh, S.4


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