메뉴 건너뛰기




Volumn 124, Issue 16, 2011, Pages 2735-2742

Bacterial genotoxin triggers FEN1-dependent RhoA activation, cytoskeleton remodeling and cell survival

Author keywords

Actin cytoskeleton; Cell survival; Cytolethal distending toxin; DNA damage; FEN1; RhoA; TSG101

Indexed keywords

ACTIN; CYTOLETHAL DISTENDING TOXIN; CYTOLETHAL DISTENDING TOXIN B; DNA; FEN1 PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; TUMOR SUSCEPTIBILITY GENE 101 PROTEIN; UNCLASSIFIED DRUG;

EID: 79961160914     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.085845     Document Type: Article
Times cited : (27)

References (52)
  • 1
    • 16844379381 scopus 로고    scopus 로고
    • PAK1 negatively regulates the activity of the Rho exchange factor NET1
    • Alberts, A. S., Qin, H., Carr, H. S. and Frost, J. A. (2005). PAK1 negatively regulates the activity of the Rho exchange factor NET1. J. Biol. Chem. 280, 12152-12161.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12152-12161
    • Alberts, A.S.1    Qin, H.2    Carr, H.S.3    Frost, J.A.4
  • 3
    • 14744289370 scopus 로고    scopus 로고
    • Par-3 controls tight junction assembly through the Rac exchange factor Tiam1
    • Chen, X. and Macara, I. G. (2005). Par-3 controls tight junction assembly through the Rac exchange factor Tiam1. Nat. Cell Biol. 7, 262-269.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 262-269
    • Chen, X.1    Macara, I.G.2
  • 5
    • 0032893106 scopus 로고    scopus 로고
    • The cytolethal distending toxin from the chancroid bacterium Haemophilus ducreyi induces cell-cycle arrest in the G2 phase
    • Cortes-Bratti, X., Chaves-Olarte, E., Lagergård, T. and Thelestam, M. (1999). The cytolethal distending toxin from the chancroid bacterium Haemophilus ducreyi induces cell-cycle arrest in the G2 phase. J. Clin. Invest. 103, 107-115.
    • (1999) J. Clin. Invest. , vol.103 , pp. 107-115
    • Cortes-Bratti, X.1    Chaves-Olarte, E.2    Lagergård, T.3    Thelestam, M.4
  • 6
    • 0035895984 scopus 로고    scopus 로고
    • The Haemophilus ducreyi cytolethal distending toxin induces cell cycle arrest and apoptosis via the DNA damage checkpoint pathways
    • Cortes-Bratti, X., Karlsson, C., Lagergard, T., Thelestam, M. and Frisan, T. (2001). The Haemophilus ducreyi cytolethal distending toxin induces cell cycle arrest and apoptosis via the DNA damage checkpoint pathways. J. Biol. Chem. 276, 5296-5302.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5296-5302
    • Cortes-Bratti, X.1    Karlsson, C.2    Lagergard, T.3    Thelestam, M.4    Frisan, T.5
  • 7
    • 13244262969 scopus 로고    scopus 로고
    • Helicobacter infection, chronic inflammation, and the development of malignancy
    • Crowe, S. E. (2005). Helicobacter infection, chronic inflammation, and the development of malignancy. Curr. Opin. Gastroenterol. 21, 32-38.
    • (2005) Curr. Opin. Gastroenterol. , vol.21 , pp. 32-38
    • Crowe, S.E.1
  • 9
    • 21744432683 scopus 로고    scopus 로고
    • GDIs: central regulatory molecules in Rho GTPase activation
    • DerMardirossian, C. and Bokoch, G. M. (2005). GDIs: central regulatory molecules in Rho GTPase activation. Trends Cell Biol. 15, 356-363.
    • (2005) Trends Cell Biol , vol.15 , pp. 356-363
    • DerMardirossian, C.1    Bokoch, G.M.2
  • 10
    • 0035058434 scopus 로고    scopus 로고
    • Escherichia coli CdtB mediates cytolethal distending toxin cell cycle arrest
    • Elwell, C., Chao, K., Patel, K. and Dreyfus, L. (2001). Escherichia coli CdtB mediates cytolethal distending toxin cell cycle arrest. Infect. Immun. 69, 3418-3422.
    • (2001) Infect. Immun. , vol.69 , pp. 3418-3422
    • Elwell, C.1    Chao, K.2    Patel, K.3    Dreyfus, L.4
  • 11
    • 33847154529 scopus 로고    scopus 로고
    • Cell polarity protein Par3 complexes with DNA-PK via Ku70 and regulates DNA double-strand break repair
    • Fang, L., Wang, Y., Du, D., Yang, G., Tak Kwok, T., Kai Kong, S., Chen, B., Chen, D. J. and Chen, Z. (2007). Cell polarity protein Par3 complexes with DNA-PK via Ku70 and regulates DNA double-strand break repair. Cell Res. 17, 100-116.
    • (2007) Cell Res , vol.17 , pp. 100-116
    • Fang, L.1    Wang, Y.2    Du, D.3    Yang, G.4    Tak Kwok, T.5    Kai Kong, S.6    Chen, B.7    Chen, D.J.8    Chen, Z.9
  • 12
    • 4644359805 scopus 로고    scopus 로고
    • Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase
    • Feng, J., Park, J., Cron, P., Hess, D. and Hemmings, B. A. (2004). Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase. J. Biol. Chem. 279, 41189-41196.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41189-41196
    • Feng, J.1    Park, J.2    Cron, P.3    Hess, D.4    Hemmings, B.A.5
  • 13
    • 0141725786 scopus 로고    scopus 로고
    • The Haemophilus ducreyi cytolethal distending toxin induces DNA double strand breaks and promotes ATM-dependent activation of RhoA
    • Frisan, T., Cortes-Bratti, X., Chaves-Olarte, E., Stenerlöw, B. and Thelestam, M. (2003). The Haemophilus ducreyi cytolethal distending toxin induces DNA double strand breaks and promotes ATM-dependent activation of RhoA. Cell. Microbiol. 5, 695-707.
    • (2003) Cell. Microbiol. , vol.5 , pp. 695-707
    • Frisan, T.1    Cortes-Bratti, X.2    Chaves-Olarte, E.3    Stenerlöw, B.4    Thelestam, M.5
  • 14
    • 0034953016 scopus 로고    scopus 로고
    • The role of different protein components from the Haemophilus ducreyi cytolethal distending toxin in the generation of cell toxicity
    • Frisk, A., Lebens, M., Johansson, C., Ahmed, H., Svensson, L., Ahlman, K. and Lagergård, T. (2001). The role of different protein components from the Haemophilus ducreyi cytolethal distending toxin in the generation of cell toxicity. Microb. Pathog. 30, 313-324.
    • (2001) Microb. Pathog. , vol.30 , pp. 313-324
    • Frisk, A.1    Lebens, M.2    Johansson, C.3    Ahmed, H.4    Svensson, L.5    Ahlman, K.6    Lagergård, T.7
  • 15
    • 0032722556 scopus 로고    scopus 로고
    • Cytolethal distending toxin of Haemophilus ducreyi induces apoptotic death of Jurkat T cells
    • Gelfanova, V., Hansen, E. J. and Spinola, S. M. (1999). Cytolethal distending toxin of Haemophilus ducreyi induces apoptotic death of Jurkat T cells. Infect. Immun. 67, 6394-6402.
    • (1999) Infect. Immun. , vol.67 , pp. 6394-6402
    • Gelfanova, V.1    Hansen, E.J.2    Spinola, S.M.3
  • 16
    • 48249149894 scopus 로고    scopus 로고
    • A bacterial cytotoxin identifies the RhoA exchange factor Net1 as a key effector in the response to DNA damage
    • Guerra, L., Carr, H. S., Richter-Dahlfors, A., Masucci, M. G., Thelestam, M., Frost, J. A. and Frisan, T. (2008a). A bacterial cytotoxin identifies the RhoA exchange factor Net1 as a key effector in the response to DNA damage. PLoS ONE 3, e2254.
    • (2008) PLoS ONE , vol.3
    • Guerra, L.1    Carr, H.S.2    Richter-Dahlfors, A.3    Masucci, M.G.4    Thelestam, M.5    Frost, J.A.6    Frisan, T.7
  • 18
    • 40449120350 scopus 로고    scopus 로고
    • An oncogene-induced DNA damage model for cancer development
    • Halazonetis, T. D., Gorgoulis, V. G. and Bartek, J. (2008). An oncogene-induced DNA damage model for cancer development. Science 319, 1352-1355.
    • (2008) Science , vol.319 , pp. 1352-1355
    • Halazonetis, T.D.1    Gorgoulis, V.G.2    Bartek, J.3
  • 19
    • 0034876258 scopus 로고    scopus 로고
    • Cytolethal distending toxin demonstrates genotoxic activity in a yeast model
    • Hassane, D. C., Lee, R. B., Mendenhall, M. D. and Pickett, C. L. (2001). Cytolethal distending toxin demonstrates genotoxic activity in a yeast model. Infect. Immun. 69, 5752-5759.
    • (2001) Infect. Immun. , vol.69 , pp. 5752-5759
    • Hassane, D.C.1    Lee, R.B.2    Mendenhall, M.D.3    Pickett, C.L.4
  • 20
    • 0037219984 scopus 로고    scopus 로고
    • Campylobacter jejuni cytolethal distending toxin promotes DNA repair responses in normal human cells
    • Hassane, D. C., Lee, R. B. and Pickett, C. L. (2003). Campylobacter jejuni cytolethal distending toxin promotes DNA repair responses in normal human cells. Infect. Immun. 71, 541-545.
    • (2003) Infect. Immun. , vol.71 , pp. 541-545
    • Hassane, D.C.1    Lee, R.B.2    Pickett, C.L.3
  • 21
    • 14744305134 scopus 로고    scopus 로고
    • Pars and polarity: taking control of Rac
    • Hurd, T. W. and Margolis, B. (2005). Pars and polarity: taking control of Rac. Nat. Cell Biol. 7, 205-207.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 205-207
    • Hurd, T.W.1    Margolis, B.2
  • 22
    • 75549090213 scopus 로고    scopus 로고
    • KEGG for representation and analysis of molecular networks involving diseases and drugs
    • Kanehisa, M., Goto, S., Furumichi, M., Tanabe, M. and Hirakawa, M. (2010). KEGG for representation and analysis of molecular networks involving diseases and drugs. Nucleic Acids Res. 38, D355-D360.
    • (2010) Nucleic Acids Res , vol.38
    • Kanehisa, M.1    Goto, S.2    Furumichi, M.3    Tanabe, M.4    Hirakawa, M.5
  • 23
    • 9244251125 scopus 로고    scopus 로고
    • Cell-cycle checkpoints and cancer
    • Kastan, M. B. and Bartek, J. (2004). Cell-cycle checkpoints and cancer. Nature 432, 316-323.
    • (2004) Nature , vol.432 , pp. 316-323
    • Kastan, M.B.1    Bartek, J.2
  • 24
    • 33847747460 scopus 로고    scopus 로고
    • Genome-wide analysis of cellular response to bacterial genotoxin CdtB in yeast
    • Kitagawa, T., Hoshida, H. and Akada, R. (2007). Genome-wide analysis of cellular response to bacterial genotoxin CdtB in yeast. Infect. Immun. 75, 1393-1402.
    • (2007) Infect. Immun. , vol.75 , pp. 1393-1402
    • Kitagawa, T.1    Hoshida, H.2    Akada, R.3
  • 25
    • 0034644631 scopus 로고    scopus 로고
    • A bacterial toxin that controls cell cycle progression as a deoxyribonuclease I-like protein
    • Lara-Tejero, M. and Galan, J. E. (2000). A bacterial toxin that controls cell cycle progression as a deoxyribonuclease I-like protein. Science 290, 354-357.
    • (2000) Science , vol.290 , pp. 354-357
    • Lara-Tejero, M.1    Galan, J.E.2
  • 26
    • 0034967972 scopus 로고    scopus 로고
    • CdtA, CdtB and CdtC form a tripartite complex that is required for cytolethal distending toxin activity
    • Lara-Tejero, M. and Galan, J. E. (2001). CdtA, CdtB and CdtC form a tripartite complex that is required for cytolethal distending toxin activity. Infect. Immun. 69, 4358-4365.
    • (2001) Infect. Immun. , vol.69 , pp. 4358-4365
    • Lara-Tejero, M.1    Galan, J.E.2
  • 27
    • 15944390635 scopus 로고    scopus 로고
    • Bacterial toxins and cancer - a case to answer?
    • Lax, A. J. (2005). Bacterial toxins and cancer - a case to answer? Nat. Rev. Microbiol. 3, 343-349.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 343-349
    • Lax, A.J.1
  • 28
    • 0041322857 scopus 로고    scopus 로고
    • Interactions of Campylobacter jejuni cytolethal distending toxin subunits CdtA and CdtC with HeLa cells
    • Lee, R. B., Hassane, D. C., Cottle, D. L. and Pickett, C. L. (2003). Interactions of Campylobacter jejuni cytolethal distending toxin subunits CdtA and CdtC with HeLa cells. Infect. Immun. 71, 4883-4890.
    • (2003) Infect. Immun. , vol.71 , pp. 4883-4890
    • Lee, R.B.1    Hassane, D.C.2    Cottle, D.L.3    Pickett, C.L.4
  • 29
    • 34047129731 scopus 로고    scopus 로고
    • The double (strand break) life of Par-3
    • Lees-Miller, S. P. (2007). The double (strand break) life of Par-3. Nat. Cell Biol. 9, 363-365.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 363-365
    • Lees-Miller, S.P.1
  • 30
    • 0036123023 scopus 로고    scopus 로고
    • The Haemophilus ducreyi cytolethal distending toxin activates sensors of DNA damage and repair complexes in proliferating and non-proliferating cells
    • Li, L., Sharipo, A., Chaves-Olarte, E., Masucci, M. G., Levitsky, V., Thelestam, M. and Frisan, T. (2002). The Haemophilus ducreyi cytolethal distending toxin activates sensors of DNA damage and repair complexes in proliferating and non-proliferating cells. Cell. Microbiol. 4, 87-99.
    • (2002) Cell. Microbiol. , vol.4 , pp. 87-99
    • Li, L.1    Sharipo, A.2    Chaves-Olarte, E.3    Masucci, M.G.4    Levitsky, V.5    Thelestam, M.6    Frisan, T.7
  • 31
    • 3943086339 scopus 로고    scopus 로고
    • Flap endonuclease 1, a central component of DNA metabolism
    • Liu, Y., Kao, H. I. and Bambara, R. A. (2004). Flap endonuclease 1, a central component of DNA metabolism. Annu. Rev. Biochem. 73, 589-615.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 589-615
    • Liu, Y.1    Kao, H.I.2    Bambara, R.A.3
  • 32
    • 0038496905 scopus 로고    scopus 로고
    • Novel localization of the DNA-PK complex in lipid rafts: a putative role in the signal transduction pathway of the ionizing radiation response
    • Lucero, H., Gae, D. and Taccioli, G. E. (2003). Novel localization of the DNA-PK complex in lipid rafts: a putative role in the signal transduction pathway of the ionizing radiation response. J. Biol. Chem. 278, 22136-22143.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22136-22143
    • Lucero, H.1    Gae, D.2    Taccioli, G.E.3
  • 33
    • 1842840103 scopus 로고    scopus 로고
    • Nuclear localization of the Escherichia coli cytolethal distending toxin CdtB subunit
    • McSweeney, L. A. and Dreyfus, L. A. (2004). Nuclear localization of the Escherichia coli cytolethal distending toxin CdtB subunit. Cell. Microbiol. 6, 447-458.
    • (2004) Cell. Microbiol. , vol.6 , pp. 447-458
    • McSweeney, L.A.1    Dreyfus, L.A.2
  • 34
    • 16244386487 scopus 로고    scopus 로고
    • Carbohydrate-binding specificity of the Escherichia coli cytolethal distending toxin CdtA-II and CdtC-II subunits
    • McSweeney, L. A. and Dreyfus, L. A. (2005). Carbohydrate-binding specificity of the Escherichia coli cytolethal distending toxin CdtA-II and CdtC-II subunits. Infect. Immun. 73, 2051-2060.
    • (2005) Infect. Immun. , vol.73 , pp. 2051-2060
    • McSweeney, L.A.1    Dreyfus, L.A.2
  • 35
    • 1242317038 scopus 로고    scopus 로고
    • NMR solution structure of the mitochondrial F1beta presequence from Nicotiana plumbaginifolia
    • Moberg, P., Nilsson, S., Stahl, A., Eriksson, A. C., Glaser, E. and Maler, L. (2004). NMR solution structure of the mitochondrial F1beta presequence from Nicotiana plumbaginifolia. J. Mol. Biol. 336, 1129-1140.
    • (2004) J. Mol. Biol. , vol.336 , pp. 1129-1140
    • Moberg, P.1    Nilsson, S.2    Stahl, A.3    Eriksson, A.C.4    Glaser, E.5    Maler, L.6
  • 36
    • 34948911522 scopus 로고    scopus 로고
    • Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis
    • Morita, E., Sandrin, V., Chung, H. Y., Morham, S. G., Gygi, S. P., Rodesch, C. K. and Sundquist, W. I. (2007). Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis. EMBO J. 26, 4215-4227.
    • (2007) EMBO J , vol.26 , pp. 4215-4227
    • Morita, E.1    Sandrin, V.2    Chung, H.Y.3    Morham, S.G.4    Gygi, S.P.5    Rodesch, C.K.6    Sundquist, W.I.7
  • 37
    • 18944377963 scopus 로고    scopus 로고
    • The double life of the Ku protein: facing the DNA breaks and the extracellular environment
    • Muller, C., Paupert, J., Monferran, S. and Salles, B. (2005). The double life of the Ku protein: facing the DNA breaks and the extracellular environment. Cell Cycle 4, 438-441.
    • (2005) Cell Cycle , vol.4 , pp. 438-441
    • Muller, C.1    Paupert, J.2    Monferran, S.3    Salles, B.4
  • 38
    • 2642550772 scopus 로고    scopus 로고
    • Assembly and function of a bacterial genotoxin
    • Nesic, D., Hsu, Y. and Stebbins, C. E. (2004). Assembly and function of a bacterial genotoxin. Nature 429, 429-433.
    • (2004) Nature , vol.429 , pp. 429-433
    • Nesic, D.1    Hsu, Y.2    Stebbins, C.E.3
  • 40
    • 13444256478 scopus 로고    scopus 로고
    • Inparanoid: a comprehensive database of eukaryotic orthologs
    • O'Brien, K. P., Remm, M. and Sonnhammer, E. L. (2005). Inparanoid: a comprehensive database of eukaryotic orthologs. Nucleic Acids Res. 33, D476-D480.
    • (2005) Nucleic Acids Res , vol.33
    • O'Brien, K.P.1    Remm, M.2    Sonnhammer, E.L.3
  • 41
    • 0037925454 scopus 로고    scopus 로고
    • CRN-1, a Caenorhabditis elegans FEN-1 homologue, cooperates with CPS-6/EndoG to promote apoptotic DNA degradation
    • Parrish, J. Z., Yang, C., Shen, B. and Xue, D. (2003). CRN-1, a Caenorhabditis elegans FEN-1 homologue, cooperates with CPS-6/EndoG to promote apoptotic DNA degradation. EMBO J. 22, 3451-3460.
    • (2003) EMBO J , vol.22 , pp. 3451-3460
    • Parrish, J.Z.1    Yang, C.2    Shen, B.3    Xue, D.4
  • 42
    • 0035896003 scopus 로고    scopus 로고
    • Cell cycle-dependent and DNA damage-inducible nuclear localization of FEN-1 nuclease is consistent with its dual functions in DNA replication and repair
    • Qiu, J., Li, X., Frank, G. and Shen, B. (2001). Cell cycle-dependent and DNA damage-inducible nuclear localization of FEN-1 nuclease is consistent with its dual functions in DNA replication and repair. J. Biol. Chem. 276, 4901-4908.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4901-4908
    • Qiu, J.1    Li, X.2    Frank, G.3    Shen, B.4
  • 43
    • 20344384024 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated protein quality control and degradation: screen for ERAD mutants after ethylmethane sulfonate mutagenesis
    • Schafer, A. and Wolf, D. H. (2005). Endoplasmic reticulum-associated protein quality control and degradation: screen for ERAD mutants after ethylmethane sulfonate mutagenesis. Methods Mol. Biol. 301, 283-288.
    • (2005) Methods Mol. Biol. , vol.301 , pp. 283-288
    • Schafer, A.1    Wolf, D.H.2
  • 44
    • 0028054721 scopus 로고
    • Cloning and sequencing of the genes encoding Escherichia coli cytolethal distending toxins
    • Scott, D. A. and Kaper, J. B. (1994). Cloning and sequencing of the genes encoding Escherichia coli cytolethal distending toxins. Infect. Immun. 62, 244-251.
    • (1994) Infect. Immun. , vol.62 , pp. 244-251
    • Scott, D.A.1    Kaper, J.B.2
  • 45
    • 0037365789 scopus 로고    scopus 로고
    • ATM and related protein kinases: safeguarding genome integrity
    • Shiloh, Y. (2003). ATM and related protein kinases: safeguarding genome integrity. Nat. Rev. Cancer 3, 155-168.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 155-168
    • Shiloh, Y.1
  • 46
    • 33845222309 scopus 로고    scopus 로고
    • The contribution of cytolethal distending toxin to bacterial pathogenesis
    • Smith, J. L. and Bayles, D. O. (2006). The contribution of cytolethal distending toxin to bacterial pathogenesis. Crit. Rev. Microbiol. 32, 227-248.
    • (2006) Crit. Rev. Microbiol. , vol.32 , pp. 227-248
    • Smith, J.L.1    Bayles, D.O.2
  • 48
    • 35548969432 scopus 로고    scopus 로고
    • DNA-dependent protein kinase in nonhomologous end joining: a lock with multiple keys? J
    • Weterings, E. and Chen, D. J. (2007). DNA-dependent protein kinase in nonhomologous end joining: a lock with multiple keys? J. Cell Biol. 179, 183-186.
    • (2007) Cell Biol , vol.179 , pp. 183-186
    • Weterings, E.1    Chen, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.