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Volumn 14, Issue 2, 2012, Pages 255-273

The Type VI secretion system of Burkholderia cenocepacia affects multiple Rho family GTPases disrupting the actin cytoskeleton and the assembly of NADPH oxidase complex in macrophages

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; COFILIN; RAC1 PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 84856026465     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/j.1462-5822.2011.01716.x     Document Type: Article
Times cited : (60)

References (77)
  • 3
    • 79959213985 scopus 로고    scopus 로고
    • Bacterial protein toxins that modify host regulatory GTPases
    • Aktories, K. (2011) Bacterial protein toxins that modify host regulatory GTPases. Nat Rev Microbiol 9: 487-498.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 487-498
    • Aktories, K.1
  • 5
    • 42949164547 scopus 로고    scopus 로고
    • A novel sensor kinase-response regulator hybrid controls biofilm formation and type VI secretion system activity in Burkholderia cenocepacia
    • Aubert, D.F., Flannagan, R.S., and Valvano, M.A. (2008) A novel sensor kinase-response regulator hybrid controls biofilm formation and type VI secretion system activity in Burkholderia cenocepacia. Infect Immun 76: 1979-1991.
    • (2008) Infect Immun , vol.76 , pp. 1979-1991
    • Aubert, D.F.1    Flannagan, R.S.2    Valvano, M.A.3
  • 7
    • 78649373184 scopus 로고    scopus 로고
    • Roles of ADF/cofilin in actin polymerization and beyond
    • Bamburg, J.R., and Bernstein, B.W. (2010) Roles of ADF/cofilin in actin polymerization and beyond. F1000 Biol Rep 2: 62.
    • (2010) F1000 Biol Rep , vol.2 , pp. 62
    • Bamburg, J.R.1    Bernstein, B.W.2
  • 8
    • 0033531955 scopus 로고    scopus 로고
    • Characterization of rac and cdc42 activation in chemoattractant-stimulated human neutrophils using a novel assay for active GTPases
    • Benard, V., Bohl, B.P., and Bokoch, G.M. (1999) Characterization of rac and cdc42 activation in chemoattractant-stimulated human neutrophils using a novel assay for active GTPases. J Biol Chem 274: 13198-13204.
    • (1999) J Biol Chem , vol.274 , pp. 13198-13204
    • Benard, V.1    Bohl, B.P.2    Bokoch, G.M.3
  • 9
    • 77950859278 scopus 로고    scopus 로고
    • ADF/cofilin: a functional node in cell biology
    • Bernstein, B.W., and Bamburg, J.R. (2010) ADF/cofilin: a functional node in cell biology. Trends Cell Biol 20: 187-195.
    • (2010) Trends Cell Biol , vol.20 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 10
    • 10344262906 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton: an oncogenic function for CDK inhibitors?
    • Besson, A., Assoian, R.K., and Roberts, J.M. (2004) Regulation of the cytoskeleton: an oncogenic function for CDK inhibitors? Nat Rev Cancer 4: 948-955.
    • (2004) Nat Rev Cancer , vol.4 , pp. 948-955
    • Besson, A.1    Assoian, R.K.2    Roberts, J.M.3
  • 11
    • 73449107179 scopus 로고    scopus 로고
    • Burkholderia mallei cluster 1 type VI secretion mutants exhibit growth and actin polymerization defects in RAW 264.7 murine macrophages
    • Burtnick, M.N., DeShazer, D., Nair, V., Gherardini, F.C., and Brett, P.J. (2010) Burkholderia mallei cluster 1 type VI secretion mutants exhibit growth and actin polymerization defects in RAW 264.7 murine macrophages. Infect Immun 78: 88-99.
    • (2010) Infect Immun , vol.78 , pp. 88-99
    • Burtnick, M.N.1    DeShazer, D.2    Nair, V.3    Gherardini, F.C.4    Brett, P.J.5
  • 12
    • 33646362299 scopus 로고    scopus 로고
    • Exopolysaccharides from Burkholderia cenocepacia inhibit neutrophil chemotaxis and scavenge reactive oxygen species
    • Bylund, J., Burgess, L.A., Cescutti, P., Ernst, R.K., and Speert, D.P. (2006) Exopolysaccharides from Burkholderia cenocepacia inhibit neutrophil chemotaxis and scavenge reactive oxygen species. J Biol Chem 281: 2526-2532.
    • (2006) J Biol Chem , vol.281 , pp. 2526-2532
    • Bylund, J.1    Burgess, L.A.2    Cescutti, P.3    Ernst, R.K.4    Speert, D.P.5
  • 13
    • 3342959166 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum utilizes multiple host evasion mechanisms to thwart NADPH oxidase-mediated killing during neutrophil infection
    • Carlyon, J.A., Abdel-Latif, D., Pypaert, M., Lacy, P., and Fikrig, E. (2004) Anaplasma phagocytophilum utilizes multiple host evasion mechanisms to thwart NADPH oxidase-mediated killing during neutrophil infection. Infect Immun 72: 4772-4783.
    • (2004) Infect Immun , vol.72 , pp. 4772-4783
    • Carlyon, J.A.1    Abdel-Latif, D.2    Pypaert, M.3    Lacy, P.4    Fikrig, E.5
  • 14
    • 48649107476 scopus 로고    scopus 로고
    • The type VI secretion toolkit
    • Cascales, E. (2008) The type VI secretion toolkit. EMBO Rep 9: 735-741.
    • (2008) EMBO Rep , vol.9 , pp. 735-741
    • Cascales, E.1
  • 15
    • 0024447719 scopus 로고
    • Heterogeneity of hematopoietic cells immortalized by v-myc/v-raf recombinant retrovirus infection of bone marrow or fetal liver
    • Cox, G.W., Mathieson, B.J., Gandino, L., Blasi, E., Radzioch, D., and Varesio, L. (1989) Heterogeneity of hematopoietic cells immortalized by v-myc/v-raf recombinant retrovirus infection of bone marrow or fetal liver. J Natl Cancer Inst 81: 1492-1496.
    • (1989) J Natl Cancer Inst , vol.81 , pp. 1492-1496
    • Cox, G.W.1    Mathieson, B.J.2    Gandino, L.3    Blasi, E.4    Radzioch, D.5    Varesio, L.6
  • 16
    • 0024446387 scopus 로고
    • A plasmid which can be transferred between Escherichia coli and Pasteurella haemolytica by electroporation and conjugation
    • Craig, F.F., Coote, J.G., Parton, R., Freer, J.H., and Gilmour, N.J. (1989) A plasmid which can be transferred between Escherichia coli and Pasteurella haemolytica by electroporation and conjugation. J Gen Microbiol 135: 2885-2890.
    • (1989) J Gen Microbiol , vol.135 , pp. 2885-2890
    • Craig, F.F.1    Coote, J.G.2    Parton, R.3    Freer, J.H.4    Gilmour, N.J.5
  • 17
    • 0032741371 scopus 로고    scopus 로고
    • NADPH oxidase activation and assembly during phagocytosis
    • DeLeo, F.R., Allen, L.A., Apicella, M., and Nauseef, W.M. (1999) NADPH oxidase activation and assembly during phagocytosis. J Immunol 163: 6732-6740.
    • (1999) J Immunol , vol.163 , pp. 6732-6740
    • DeLeo, F.R.1    Allen, L.A.2    Apicella, M.3    Nauseef, W.M.4
  • 18
    • 77951474502 scopus 로고    scopus 로고
    • A bacterial effector targets host DH-PH domain RhoGEFs and antagonizes macrophage phagocytosis
    • Dong, N., Liu, L., and Shao, F. (2010) A bacterial effector targets host DH-PH domain RhoGEFs and antagonizes macrophage phagocytosis. EMBO J 29: 1363-1376.
    • (2010) EMBO J , vol.29 , pp. 1363-1376
    • Dong, N.1    Liu, L.2    Shao, F.3
  • 19
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville, S., and Hall, A. (2002) Rho GTPases in cell biology. Nature 420: 629-635.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 20
    • 43449100659 scopus 로고    scopus 로고
    • A system for the construction of targeted unmarked gene deletions in the genus Burkholderia
    • Flannagan, R.S., Linn, T., and Valvano, M.A. (2008) A system for the construction of targeted unmarked gene deletions in the genus Burkholderia. Environ Microbiol 10: 1652-1660.
    • (2008) Environ Microbiol , vol.10 , pp. 1652-1660
    • Flannagan, R.S.1    Linn, T.2    Valvano, M.A.3
  • 21
    • 64749091309 scopus 로고    scopus 로고
    • Antimicrobial mechanisms of phagocytes and bacterial evasion strategies
    • Flannagan, R.S., Cosio, G., and Grinstein, S. (2009) Antimicrobial mechanisms of phagocytes and bacterial evasion strategies. Nat Rev Microbiol 7: 355-366.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 355-366
    • Flannagan, R.S.1    Cosio, G.2    Grinstein, S.3
  • 23
    • 77957812911 scopus 로고    scopus 로고
    • Polarization and migration of hematopoietic stem and progenitor cells rely on the RhoA/ROCK I pathway and an active reorganization of the microtubule network
    • Fonseca, A.V., Freund, D., Bornhauser, M., and Corbeil, D. (2010) Polarization and migration of hematopoietic stem and progenitor cells rely on the RhoA/ROCK I pathway and an active reorganization of the microtubule network. J Biol Chem 285: 31661-31671.
    • (2010) J Biol Chem , vol.285 , pp. 31661-31671
    • Fonseca, A.V.1    Freund, D.2    Bornhauser, M.3    Corbeil, D.4
  • 24
    • 0033575956 scopus 로고    scopus 로고
    • A salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
    • Fu, Y., and Galan, J.E. (1999) A salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 401: 293-297.
    • (1999) Nature , vol.401 , pp. 293-297
    • Fu, Y.1    Galan, J.E.2
  • 25
    • 0028906471 scopus 로고
    • Function of wild-type or mutant Rac2 and Rap1a GTPases in differentiated HL60 cell NADPH oxidase activation
    • Gabig, T.G., Crean, C.D., Mantel, P.L., and Rosli, R. (1995) Function of wild-type or mutant Rac2 and Rap1a GTPases in differentiated HL60 cell NADPH oxidase activation. Blood 85: 804-811.
    • (1995) Blood , vol.85 , pp. 804-811
    • Gabig, T.G.1    Crean, C.D.2    Mantel, P.L.3    Rosli, R.4
  • 26
    • 77649222989 scopus 로고    scopus 로고
    • Rac1 inactivation by lethal toxin from Clostridium sordellii modifies focal adhesions upstream of actin depolymerization
    • Geny, B., Grassart, A., Manich, M., Chicanne, G., Payrastre, B., Sauvonnet, N., and Popoff, M.R. (2010) Rac1 inactivation by lethal toxin from Clostridium sordellii modifies focal adhesions upstream of actin depolymerization. Cell Microbiol 12: 217-232.
    • (2010) Cell Microbiol , vol.12 , pp. 217-232
    • Geny, B.1    Grassart, A.2    Manich, M.3    Chicanne, G.4    Payrastre, B.5    Sauvonnet, N.6    Popoff, M.R.7
  • 27
    • 0034704120 scopus 로고    scopus 로고
    • Targeting of Rac1 to the phagocyte membrane is sufficient for the induction of NADPH oxidase assembly
    • Gorzalczany, Y., Sigal, N., Itan, M., Lotan, O., and Pick, E. (2000) Targeting of Rac1 to the phagocyte membrane is sufficient for the induction of NADPH oxidase assembly. J Biol Chem 275: 40073-40081.
    • (2000) J Biol Chem , vol.275 , pp. 40073-40081
    • Gorzalczany, Y.1    Sigal, N.2    Itan, M.3    Lotan, O.4    Pick, E.5
  • 28
    • 15944372262 scopus 로고    scopus 로고
    • Activation and assembly of the NADPH oxidase: a structural perspective
    • Groemping, Y., and Rittinger, K. (2005) Activation and assembly of the NADPH oxidase: a structural perspective. Biochem J 386: 401-416.
    • (2005) Biochem J , vol.386 , pp. 401-416
    • Groemping, Y.1    Rittinger, K.2
  • 29
    • 77950481822 scopus 로고    scopus 로고
    • Sequestering of Rac by the Yersinia effector YopO blocks Fcγ receptor-mediated phagocytosis
    • Groves, E., Rittinger, K., Amstutz, M., Berry, S., Holden, D.W., Cornelis, G.R., and Caron, E. (2010) Sequestering of Rac by the Yersinia effector YopO blocks Fcγ receptor-mediated phagocytosis. J Biol Chem 285: 4087-4098.
    • (2010) J Biol Chem , vol.285 , pp. 4087-4098
    • Groves, E.1    Rittinger, K.2    Amstutz, M.3    Berry, S.4    Holden, D.W.5    Cornelis, G.R.6    Caron, E.7
  • 30
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. (1998) Rho GTPases and the actin cytoskeleton. Science 279: 509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 31
    • 37549037453 scopus 로고    scopus 로고
    • Evasion of Legionella pneumophila from the bactericidal system by reactive oxygen species (ROS) in macrophages
    • Harada, T., Miyake, M., and Imai, Y. (2007) Evasion of Legionella pneumophila from the bactericidal system by reactive oxygen species (ROS) in macrophages. Microbiol Immunol 51: 1161-1170.
    • (2007) Microbiol Immunol , vol.51 , pp. 1161-1170
    • Harada, T.1    Miyake, M.2    Imai, Y.3
  • 32
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: new insights into their functions from in vivo studies
    • Heasman, S.J., and Ridley, A.J. (2008) Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat Rev Mol Cell Biol 9: 690-701.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 33
    • 77955887642 scopus 로고    scopus 로고
    • Coordinated RhoA signaling at the leading edge and uropod is required for T cell transendothelial migration
    • Heasman, S.J., Carlin, L.M., Cox, S., Ng, T., and Ridley, A.J. (2010) Coordinated RhoA signaling at the leading edge and uropod is required for T cell transendothelial migration. J Cell Biol 190: 553-563.
    • (2010) J Cell Biol , vol.190 , pp. 553-563
    • Heasman, S.J.1    Carlin, L.M.2    Cox, S.3    Ng, T.4    Ridley, A.J.5
  • 35
    • 3042601400 scopus 로고    scopus 로고
    • Identification of Burkholderia cenocepacia genes required for bacterial survival in vivo
    • Hunt, T.A., Kooi, C., Sokol, P.A., and Valvano, M.A. (2004) Identification of Burkholderia cenocepacia genes required for bacterial survival in vivo. Infect Immun 72: 4010-4022.
    • (2004) Infect Immun , vol.72 , pp. 4010-4022
    • Hunt, T.A.1    Kooi, C.2    Sokol, P.A.3    Valvano, M.A.4
  • 38
    • 77958182267 scopus 로고    scopus 로고
    • Type VI secretion: not just for pathogenesis anymore
    • Jani, A.J., and Cotter, P.A. (2010) Type VI secretion: not just for pathogenesis anymore. Cell Host Microbe 8: 2-6.
    • (2010) Cell Host Microbe , vol.8 , pp. 2-6
    • Jani, A.J.1    Cotter, P.A.2
  • 39
    • 77952540479 scopus 로고    scopus 로고
    • Activation of Rho GTPases in Smith-Lemli-Opitz syndrome: pathophysiological and clinical implications
    • Jiang, X.S., Wassif, C.A., Backlund, P.S., Song, L., Holtzclaw, L.A., Li, Z., etal. (2010) Activation of Rho GTPases in Smith-Lemli-Opitz syndrome: pathophysiological and clinical implications. Hum Mol Genet 19: 1347-1357.
    • (2010) Hum Mol Genet , vol.19 , pp. 1347-1357
    • Jiang, X.S.1    Wassif, C.A.2    Backlund, P.S.3    Song, L.4    Holtzclaw, L.A.5    Li, Z.6
  • 40
    • 0028288879 scopus 로고
    • Linkage analysis of geographic and clinical clusters in Pseudomonas cepacia infections by multilocus enzyme electrophoresis and ribotyping
    • Johnson, W.M., Tyler, S.D., and Rozee, K.R. (1994) Linkage analysis of geographic and clinical clusters in Pseudomonas cepacia infections by multilocus enzyme electrophoresis and ribotyping. J Clin Microbiol 32: 924-930.
    • (1994) J Clin Microbiol , vol.32 , pp. 924-930
    • Johnson, W.M.1    Tyler, S.D.2    Rozee, K.R.3
  • 41
    • 65649095938 scopus 로고    scopus 로고
    • Delayed association of the NADPH oxidase complex with macrophage vacuoles containing the opportunistic pathogen Burkholderia cenocepacia
    • Keith, K.E., Hynes, D.W., Sholdice, J.E., and Valvano, M.A. (2009) Delayed association of the NADPH oxidase complex with macrophage vacuoles containing the opportunistic pathogen Burkholderia cenocepacia. Microbiology 155: 1004-1015.
    • (2009) Microbiology , vol.155 , pp. 1004-1015
    • Keith, K.E.1    Hynes, D.W.2    Sholdice, J.E.3    Valvano, M.A.4
  • 42
    • 0027067903 scopus 로고
    • Purification and characterization of Rac 2. A cytosolic GTP-binding protein that regulates human neutrophil NADPH oxidase
    • Knaus, U.G., Heyworth, P.G., Kinsella, B.T., Curnutte, J.T., and Bokoch, G.M. (1992) Purification and characterization of Rac 2. A cytosolic GTP-binding protein that regulates human neutrophil NADPH oxidase. J Biol Chem 267: 23575-23582.
    • (1992) J Biol Chem , vol.267 , pp. 23575-23582
    • Knaus, U.G.1    Heyworth, P.G.2    Kinsella, B.T.3    Curnutte, J.T.4    Bokoch, G.M.5
  • 43
    • 58949097885 scopus 로고    scopus 로고
    • Burkholderia cenocepacia-induced delay of acidification and phagolysosomal fusion in cystic fibrosis transmembrane conductance regulator (CFTR)-defective macrophages
    • Lamothe, J., and Valvano, M.A. (2008) Burkholderia cenocepacia-induced delay of acidification and phagolysosomal fusion in cystic fibrosis transmembrane conductance regulator (CFTR)-defective macrophages. Microbiology 154: 3825-3834.
    • (2008) Microbiology , vol.154 , pp. 3825-3834
    • Lamothe, J.1    Valvano, M.A.2
  • 44
    • 33845412832 scopus 로고    scopus 로고
    • Intracellular survival of Burkholderia cenocepacia in macrophages is associated with a delay in the maturation of bacteria-containing vacuoles
    • Lamothe, J., Huynh, K.K., Grinstein, S., and Valvano, M.A. (2007) Intracellular survival of Burkholderia cenocepacia in macrophages is associated with a delay in the maturation of bacteria-containing vacuoles. Cell Microbiol 9: 40-53.
    • (2007) Cell Microbiol , vol.9 , pp. 40-53
    • Lamothe, J.1    Huynh, K.K.2    Grinstein, S.3    Valvano, M.A.4
  • 45
    • 77956020315 scopus 로고    scopus 로고
    • Regulation of actin cytoskeleton dynamics in cells
    • Lee, S.H., and Dominguez, R. (2010) Regulation of actin cytoskeleton dynamics in cells. Mol Cells 29: 311-325.
    • (2010) Mol Cells , vol.29 , pp. 311-325
    • Lee, S.H.1    Dominguez, R.2
  • 46
    • 27644445124 scopus 로고    scopus 로고
    • Update on the Burkholderia cepacia complex
    • Lipuma, J.J. (2005) Update on the Burkholderia cepacia complex. Curr Opin Pulm Med 11: 528-533.
    • (2005) Curr Opin Pulm Med , vol.11 , pp. 528-533
    • Lipuma, J.J.1
  • 47
    • 33750611352 scopus 로고    scopus 로고
    • Leishmania donovani lipophosphoglycan blocks NADPH oxidase assembly at the phagosome membrane
    • Lodge, R., Diallo, T.O., and Descoteaux, A. (2006) Leishmania donovani lipophosphoglycan blocks NADPH oxidase assembly at the phagosome membrane. Cell Microbiol 8: 1922-1931.
    • (2006) Cell Microbiol , vol.8 , pp. 1922-1931
    • Lodge, R.1    Diallo, T.O.2    Descoteaux, A.3
  • 48
    • 0034426779 scopus 로고    scopus 로고
    • A method to purify bacteria-containing phagosomes from infected macrophages
    • Luhrmann, A., and Haas, A. (2000) A method to purify bacteria-containing phagosomes from infected macrophages. Methods Cell Sci 22: 329-341.
    • (2000) Methods Cell Sci , vol.22 , pp. 329-341
    • Luhrmann, A.1    Haas, A.2
  • 49
    • 77749297949 scopus 로고    scopus 로고
    • In vivo actin cross-linking induced by Vibrio cholerae type VI secretion system is associated with intestinal inflammation
    • Ma, A.T., and Mekalanos, J.J. (2010) In vivo actin cross-linking induced by Vibrio cholerae type VI secretion system is associated with intestinal inflammation. Proc Natl Acad Sci USA 107: 4365-4370.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4365-4370
    • Ma, A.T.1    Mekalanos, J.J.2
  • 50
    • 61849114089 scopus 로고    scopus 로고
    • Translocation of a Vibrio cholerae type VI secretion effector requires bacterial endocytosis by host cells
    • Ma, A.T., McAuley, S., Pukatzki, S., and Mekalanos, J.J. (2009) Translocation of a Vibrio cholerae type VI secretion effector requires bacterial endocytosis by host cells. Cell Host Microbe 5: 234-243.
    • (2009) Cell Host Microbe , vol.5 , pp. 234-243
    • Ma, A.T.1    McAuley, S.2    Pukatzki, S.3    Mekalanos, J.J.4
  • 51
    • 0036264824 scopus 로고    scopus 로고
    • The ADF/cofilin family: actin-remodeling proteins
    • Maciver, S.K., and Hussey, P.J. (2002) The ADF/cofilin family: actin-remodeling proteins. Genome Biol 3: reviews3007.
    • (2002) Genome Biol , vol.3
    • Maciver, S.K.1    Hussey, P.J.2
  • 52
    • 0033529620 scopus 로고    scopus 로고
    • Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase
    • Maekawa, M., Ishizaki, T., Boku, S., Watanabe, N., Fujita, A., Iwamatsu, A., etal. (1999) Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 285: 895-898.
    • (1999) Science , vol.285 , pp. 895-898
    • Maekawa, M.1    Ishizaki, T.2    Boku, S.3    Watanabe, N.4    Fujita, A.5    Iwamatsu, A.6
  • 53
    • 13444251656 scopus 로고    scopus 로고
    • The multifarious, multireplicon Burkholderia cepacia complex
    • Mahenthiralingam, E., Urban, T.A., and Goldberg, J.B. (2005) The multifarious, multireplicon Burkholderia cepacia complex. Nat Rev Microbiol 3: 144-156.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 144-156
    • Mahenthiralingam, E.1    Urban, T.A.2    Goldberg, J.B.3
  • 54
    • 0036181922 scopus 로고    scopus 로고
    • Effects of Anaplasma phagocytophila on NADPH oxidase components in human neutrophils and HL-60 cells
    • Mott, J., Rikihisa, Y., and Tsunawaki, S. (2002) Effects of Anaplasma phagocytophila on NADPH oxidase components in human neutrophils and HL-60 cells. Infect Immun 70: 1359-1366.
    • (2002) Infect Immun , vol.70 , pp. 1359-1366
    • Mott, J.1    Rikihisa, Y.2    Tsunawaki, S.3
  • 55
    • 33744974779 scopus 로고    scopus 로고
    • A virulence locus of Pseudomonas aeruginosa encodes a protein secretion apparatus
    • Mougous, J.D., Cuff, M.E., Raunser, S., Shen, A., Zhou, M., Gifford, C.A., etal. (2006) A virulence locus of Pseudomonas aeruginosa encodes a protein secretion apparatus. Science 312: 1526-1530.
    • (2006) Science , vol.312 , pp. 1526-1530
    • Mougous, J.D.1    Cuff, M.E.2    Raunser, S.3    Shen, A.4    Zhou, M.5    Gifford, C.A.6
  • 56
    • 8644255770 scopus 로고    scopus 로고
    • Assembly of the phagocyte NADPH oxidase
    • Nauseef, W.M. (2004) Assembly of the phagocyte NADPH oxidase. Histochem Cell Biol 122: 277-291.
    • (2004) Histochem Cell Biol , vol.122 , pp. 277-291
    • Nauseef, W.M.1
  • 57
    • 0034602959 scopus 로고    scopus 로고
    • Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop
    • Ohashi, K., Nagata, K., Maekawa, M., Ishizaki, T., Narumiya, S., and Mizuno, K. (2000) Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop. J Biol Chem 275: 3577-3582.
    • (2000) J Biol Chem , vol.275 , pp. 3577-3582
    • Ohashi, K.1    Nagata, K.2    Maekawa, M.3    Ishizaki, T.4    Narumiya, S.5    Mizuno, K.6
  • 58
    • 71749095987 scopus 로고    scopus 로고
    • The cofilin activity cycle in lamellipodia and invadopodia
    • Oser, M., and Condeelis, J. (2009) The cofilin activity cycle in lamellipodia and invadopodia. J Cell Biochem 108: 1252-1262.
    • (2009) J Cell Biochem , vol.108 , pp. 1252-1262
    • Oser, M.1    Condeelis, J.2
  • 59
    • 33750724697 scopus 로고    scopus 로고
    • Differential activation and function of Rho GTPases during Salmonella-host cell interactions
    • Patel, J.C., and Galan, J.E. (2006) Differential activation and function of Rho GTPases during Salmonella-host cell interactions. J Cell Biol 175: 453-463.
    • (2006) J Cell Biol , vol.175 , pp. 453-463
    • Patel, J.C.1    Galan, J.E.2
  • 60
    • 0025006851 scopus 로고
    • Pseudomonas aeruginosa alginate in cystic fibrosis sputum and the inflammatory response
    • Pedersen, S.S., Kharazmi, A., Espersen, F., and Hoiby, N. (1990) Pseudomonas aeruginosa alginate in cystic fibrosis sputum and the inflammatory response. Infect Immun 58: 3363-3368.
    • (1990) Infect Immun , vol.58 , pp. 3363-3368
    • Pedersen, S.S.1    Kharazmi, A.2    Espersen, F.3    Hoiby, N.4
  • 61
    • 77953145912 scopus 로고    scopus 로고
    • Spatio-temporal Rho GTPase signaling - where are we now?
    • Pertz, O. (2010) Spatio-temporal Rho GTPase signaling - where are we now? J Cell Sci 123: 1841-1850.
    • (2010) J Cell Sci , vol.123 , pp. 1841-1850
    • Pertz, O.1
  • 62
    • 68049083547 scopus 로고    scopus 로고
    • Random versus directionally persistent cell migration
    • Petrie, R.J., Doyle, A.D., and Yamada, K.M. (2009) Random versus directionally persistent cell migration. Nat Rev Mol Cell Biol 10: 538-549.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 538-549
    • Petrie, R.J.1    Doyle, A.D.2    Yamada, K.M.3
  • 63
    • 34848882221 scopus 로고    scopus 로고
    • Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin
    • Pukatzki, S., Ma, A.T., Revel, A.T., Sturtevant, D., and Mekalanos, J.J. (2007) Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin. Proc Natl Acad Sci USA 104: 15508-15513.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 15508-15513
    • Pukatzki, S.1    Ma, A.T.2    Revel, A.T.3    Sturtevant, D.4    Mekalanos, J.J.5
  • 64
    • 59849101362 scopus 로고    scopus 로고
    • The type VI secretion system: translocation of effectors and effector-domains
    • Pukatzki, S., McAuley, S.B., and Miyata, S.T. (2009) The type VI secretion system: translocation of effectors and effector-domains. Curr Opin Microbiol 12: 11-17.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 11-17
    • Pukatzki, S.1    McAuley, S.B.2    Miyata, S.T.3
  • 65
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A.J., Paterson, H.F., Johnston, C.L., Diekmann, D., and Hall, A. (1992) The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70: 401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 66
    • 69949123399 scopus 로고    scopus 로고
    • Interactions of Burkholderia cenocepacia and other Burkholderia cepacia complex bacteria with epithelial and phagocytic cells
    • Saldías, M.S., and Valvano, M.A. (2009) Interactions of Burkholderia cenocepacia and other Burkholderia cepacia complex bacteria with epithelial and phagocytic cells. Microbiology 155: 2809-2817.
    • (2009) Microbiology , vol.155 , pp. 2809-2817
    • Saldías, M.S.1    Valvano, M.A.2
  • 67
    • 73449121106 scopus 로고    scopus 로고
    • Burkholderia cenocepacia O antigen lipopolysaccharide prevents phagocytosis by macrophages and adhesion to epithelial cells
    • Saldías, M.S., Ortega, X., and Valvano, M.A. (2009) Burkholderia cenocepacia O antigen lipopolysaccharide prevents phagocytosis by macrophages and adhesion to epithelial cells. J Med Microbiol 58: 1542-1548.
    • (2009) J Med Microbiol , vol.58 , pp. 1542-1548
    • Saldías, M.S.1    Ortega, X.2    Valvano, M.A.3
  • 68
    • 77958145264 scopus 로고    scopus 로고
    • Burkholderia type VI secretion systems have distinct roles in eukaryotic and bacterial cell interactions
    • Schwarz, S., West, T.E., Boyer, F., Chiang, W.C., Carl, M.A., Hood, R.D., etal. (2010) Burkholderia type VI secretion systems have distinct roles in eukaryotic and bacterial cell interactions. PLoS Pathog 6: e1001068.
    • (2010) PLoS Pathog , vol.6
    • Schwarz, S.1    West, T.E.2    Boyer, F.3    Chiang, W.C.4    Carl, M.A.5    Hood, R.D.6
  • 69
    • 67649213525 scopus 로고    scopus 로고
    • Inhibition of the human neutrophil NADPH oxidase by Coxiella burnetii
    • Siemsen, D.W., Kirpotina, L.N., Jutila, M.A., and Quinn, M.T. (2009) Inhibition of the human neutrophil NADPH oxidase by Coxiella burnetii. Microbes Infect 11: 671-679.
    • (2009) Microbes Infect , vol.11 , pp. 671-679
    • Siemsen, D.W.1    Kirpotina, L.N.2    Jutila, M.A.3    Quinn, M.T.4
  • 70
    • 0032879405 scopus 로고    scopus 로고
    • Stage-dependent redistribution of the V-ATPase during bovine implantation
    • Skinner, M.A., MacLaren, L.A., and Wildeman, A.G. (1999) Stage-dependent redistribution of the V-ATPase during bovine implantation. J Histochem Cytochem 47: 1247-1254.
    • (1999) J Histochem Cytochem , vol.47 , pp. 1247-1254
    • Skinner, M.A.1    MacLaren, L.A.2    Wildeman, A.G.3
  • 71
    • 77954453497 scopus 로고    scopus 로고
    • ROS-inhibitory activity of YopE is required for full virulence of Yersinia in mice
    • Songsungthong, W., Higgins, M.C., Rolan, H.G., Murphy, J.L., and Mecsas, J. (2010) ROS-inhibitory activity of YopE is required for full virulence of Yersinia in mice. Cell Microbiol 12: 988-1001.
    • (2010) Cell Microbiol , vol.12 , pp. 988-1001
    • Songsungthong, W.1    Higgins, M.C.2    Rolan, H.G.3    Murphy, J.L.4    Mecsas, J.5
  • 72
    • 73849101081 scopus 로고    scopus 로고
    • A type VI secretion system effector protein, VgrG1, from Aeromonas hydrophila that induces host cell toxicity by ADP ribosylation of actin
    • Suarez, G., Sierra, J.C., Erova, T.E., Sha, J., Horneman, A.J., and Chopra, A.K. (2010) A type VI secretion system effector protein, VgrG1, from Aeromonas hydrophila that induces host cell toxicity by ADP ribosylation of actin. J Bacteriol 192: 155-168.
    • (2010) J Bacteriol , vol.192 , pp. 155-168
    • Suarez, G.1    Sierra, J.C.2    Erova, T.E.3    Sha, J.4    Horneman, A.J.5    Chopra, A.K.6
  • 73
    • 0035808419 scopus 로고    scopus 로고
    • Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase
    • Sumi, T., Matsumoto, K., and Nakamura, T. (2001) Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase. J Biol Chem 276: 670-676.
    • (2001) J Biol Chem , vol.276 , pp. 670-676
    • Sumi, T.1    Matsumoto, K.2    Nakamura, T.3
  • 74
    • 33750897683 scopus 로고    scopus 로고
    • Regulation of novel superoxide-producing NAD(P)H oxidases
    • Takeya, R., and Sumimoto, H. (2006) Regulation of novel superoxide-producing NAD(P)H oxidases. Antioxid Redox Signal 8: 1523-1532.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1523-1532
    • Takeya, R.1    Sumimoto, H.2
  • 75
    • 0034095005 scopus 로고    scopus 로고
    • Salmonella pathogenicity island 2-dependent evasion of the phagocyte NADPH oxidase
    • Vazquez-Torres, A., Xu, Y., Jones-Carson, J., Holden, D.W., Lucia, S.M., Dinauer, M.C., etal. (2000) Salmonella pathogenicity island 2-dependent evasion of the phagocyte NADPH oxidase. Science 287: 1655-1658.
    • (2000) Science , vol.287 , pp. 1655-1658
    • Vazquez-Torres, A.1    Xu, Y.2    Jones-Carson, J.3    Holden, D.W.4    Lucia, S.M.5    Dinauer, M.C.6
  • 76
    • 0032565769 scopus 로고    scopus 로고
    • Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • Yang, N., Higuchi, O., Ohashi, K., Nagata, K., Wada, A., Kangawa, K., etal. (1998) Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 393: 809-812.
    • (1998) Nature , vol.393 , pp. 809-812
    • Yang, N.1    Higuchi, O.2    Ohashi, K.3    Nagata, K.4    Wada, A.5    Kangawa, K.6
  • 77
    • 0034658674 scopus 로고    scopus 로고
    • Oncogenic Ras downregulates Rac activity, which leads to increased Rho activity and epithelial-mesenchymal transition
    • Zondag, G.C., Evers, E.E., ten Klooster, J.P., Janssen, L., van der Kammen, R.A., and Collard, J.G. (2000) Oncogenic Ras downregulates Rac activity, which leads to increased Rho activity and epithelial-mesenchymal transition. J Cell Biol 149: 775-782.
    • (2000) J Cell Biol , vol.149 , pp. 775-782
    • Zondag, G.C.1    Evers, E.E.2    ten Klooster, J.P.3    Janssen, L.4    van der Kammen, R.A.5    Collard, J.G.6


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