메뉴 건너뛰기




Volumn 9, Issue 7, 2011, Pages 487-498

Bacterial protein toxins that modify host regulatory GTPases

Author keywords

[No Author keywords available]

Indexed keywords

ARF PROTEIN; BACTERIAL PROTEIN; BACTERIAL TOXIN; CHOLERA TOXIN; CLOSTRIDIUM DIFFICILE TOXIN A; CLOSTRIDIUM DIFFICILE TOXIN B; CYTOTOXIC NECROTIZING FACTOR 1; EXOENZYME C3; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; PERTUSSIS TOXIN; PROTEIN CDC42; RAB PROTEIN; RHO FACTOR; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; URIDINE DIPHOSPHATE;

EID: 79959213985     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro2592     Document Type: Review
Times cited : (236)

References (153)
  • 1
    • 70350509805 scopus 로고    scopus 로고
    • Intestinal mucosal barrier function in health and disease
    • Turner, J. R. Intestinal mucosal barrier function in health and disease. Nature Rev. Immunol. 9, 799-809 (2009).
    • (2009) Nature Rev. Immunol. , vol.9 , pp. 799-809
    • Turner, J.R.1
  • 2
    • 75749139748 scopus 로고    scopus 로고
    • Breaking the wall: Targeting of the endothelium by pathogenic bacteria
    • Lemichez, E., Lecuit, M., Nassif, X. & Bourdoulous, S. Breaking the wall: targeting of the endothelium by pathogenic bacteria. Nature Rev. Microbiol. 8, 93-104 (2010).
    • (2010) Nature Rev. Microbiol. , vol.8 , pp. 93-104
    • Lemichez, E.1    Lecuit, M.2    Nassif, X.3    Bourdoulous, S.4
  • 3
    • 70249116807 scopus 로고    scopus 로고
    • Actin dynamics at the leading edge: From simple machinery to complex networks
    • Insall, R. H. & Machesky, L. M. Actin dynamics at the leading edge: from simple machinery to complex networks. Dev. Cell 17, 310-322 (2009).
    • (2009) Dev. Cell , vol.17 , pp. 310-322
    • Insall, R.H.1    MacHesky, L.M.2
  • 4
    • 14744299030 scopus 로고    scopus 로고
    • Regulation of innate immunity by Rho GTPases
    • DOI 10.1016/j.tcb.2005.01.002
    • Bokoch, G. M. Regulation of innate immunity by Rho GTPases. Trends Cell Biol. 15, 163-171 (2005). (Pubitemid 40332539)
    • (2005) Trends in Cell Biology , vol.15 , Issue.3 , pp. 163-171
    • Bokoch, G.M.1
  • 5
    • 77649153819 scopus 로고    scopus 로고
    • WASP: A key immunological multitasker
    • Thrasher, A. J. & Burns, S. O. WASP: a key immunological multitasker. Nature Rev. Immunol. 10, 182-192 (2010).
    • (2010) Nature Rev. Immunol. , vol.10 , pp. 182-192
    • Thrasher, A.J.1    Burns, S.O.2
  • 6
    • 84863860582 scopus 로고    scopus 로고
    • The cytoskeleton coordinates the early events of B-cell activation
    • Harwood, N. E. & Batista, F. D. The cytoskeleton coordinates the early events of B-cell activation. Cold Spring Harb. Perspect. Biol. 3, a002360 (2010).
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.3
    • Harwood, N.E.1    Batista, F.D.2
  • 8
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. Rho GTPases and the actin cytoskeleton. Science 279, 509-514 (1998).
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 10
    • 0842281652 scopus 로고    scopus 로고
    • Rho and rac take center stage
    • DOI 10.1016/S0092-8674(04)00003-0
    • Burridge, K. & Wennerberg, K. Rho and Rac take center stage. Cell 116, 167-179 (2004). (Pubitemid 38167310)
    • (2004) Cell , vol.116 , Issue.2 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 11
    • 13444252631 scopus 로고    scopus 로고
    • GEF means go: Turning on Rho GTPases with guanine nucleotide-exchange factors
    • DOI 10.1038/nrm1587
    • Rossman, K. L., Der, C. J. & Sondek, J. GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors. Nature Rev. Mol. Cell Biol. 6, 167-180 (2005). (Pubitemid 40215811)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.2 , pp. 167-180
    • Rossman, K.L.1    Der, C.J.2    Sondek, J.3
  • 12
    • 0031970317 scopus 로고    scopus 로고
    • Membrane association and targeting of prenylated Ras-like GTPases
    • DOI 10.1016/S0898-6568(97)00120-4, PII S0898656897001204
    • Seabra, M. C. Membrane association and targeting of prenylated Ras-like GTPases. Cell. Signal. 10, 167-172 (1998). (Pubitemid 28156067)
    • (1998) Cellular Signalling , vol.10 , Issue.3 , pp. 167-172
    • Seabra, M.C.1
  • 13
    • 33846969965 scopus 로고    scopus 로고
    • Current knowledge of the large RhoGAP family of proteins
    • DOI 10.1042/BC20060086
    • Tcherkezian, J. & Lamarche-Vane, N. Current knowledge of the large RhoGAP family of proteins. Biol. Cell 99, 67-86 (2007). (Pubitemid 46242033)
    • (2007) Biology of the Cell , vol.99 , Issue.2 , pp. 67-86
    • Tcherkezian, J.1    Lamarche-Vane, N.2
  • 14
    • 21744432683 scopus 로고    scopus 로고
    • GDIs: Central regulatory molecules in Rho GTPase activation
    • DOI 10.1016/j.tcb.2005.05.001, PII S0962892405001273
    • DerMardirossian, C. & Bokoch, G. M. GDIs: central regulatory molecules in Rho GTPase activation. Trends Cell Biol. 15, 356-363 (2005). (Pubitemid 40943524)
    • (2005) Trends in Cell Biology , vol.15 , Issue.7 , pp. 356-363
    • DerMardirossian, C.1    Bokoch, G.M.2
  • 15
    • 0024584734 scopus 로고
    • The rho gene product expressed in E. coli is a substate of botulinum ADP-ribosyltransferase C3
    • DOI 10.1016/S0006-291X(89)80199-8
    • Aktories, K., Braun, U., Rösener, S., Just, I. & Hall, A. The rho gene product expressed in E. coli is a substrate of botulinum ADP-ribosyltransferase C3. Biochem. Biophys. Res. Commun. 158, 209-213 (1989). (Pubitemid 19045066)
    • (1989) Biochemical and Biophysical Research Communications , vol.158 , Issue.1 , pp. 209-213
    • Aktories, K.1    Braun, U.2    Rosener, S.3    Just, I.4    Hall, A.5
  • 16
    • 0024449589 scopus 로고
    • The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells
    • Chardin, P. et al. The mammalian G protein rho C is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilament in Vero cells. EMBO J. 8, 1087-1092 (1989). (Pubitemid 19273274)
    • (1989) EMBO Journal , vol.8 , Issue.4 , pp. 1087-1092
    • Chardin, P.1    Boquet, P.2    Madaule, P.3    Popoff, M.R.4    Rubin, E.J.5    Gill, D.M.6
  • 17
    • 17844406602 scopus 로고    scopus 로고
    • Bacterial cytotoxins: Targeting eukaryotic switches
    • DOI 10.1038/nrmicro1150
    • Aktories, K. & Barbieri, J. T. Bacterial cytotoxins: targeting eukaryotic switches. Nature Rev. Microbiol. 3, 397-410 (2005). (Pubitemid 40590382)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.5 , pp. 397-410
    • Aktories, K.1    Barbieri, J.T.2
  • 18
    • 0038062664 scopus 로고    scopus 로고
    • Bacterial virulence factors targeting Rho GTPases: Parasitism or symbiosis?
    • DOI 10.1016/S0962-8924(03)00037-0
    • Boquet, P. & Lemichez, E. Bacterial virulence factors targeting Rho GTPases: parasitism or symbiosis? Trends Cell Biol. 13, 238-246 (2003). (Pubitemid 36556008)
    • (2003) Trends in Cell Biology , vol.13 , Issue.5 , pp. 238-246
    • Boquet, P.1    Lemichez, E.2
  • 19
    • 0025195876 scopus 로고
    • Microinjection of recombinant p21rho induces rapid changes in cell morphology
    • Paterson, H. F. et al. Microinjection of recombinant p21rho induces rapid changes in cell morphology. J. Cell Biol. 111, 1001-1007 (1990).
    • (1990) J. Cell Biol. , vol.111 , pp. 1001-1007
    • Paterson, H.F.1
  • 20
    • 2142713987 scopus 로고    scopus 로고
    • Snails Swiss and serum: The solution for Rac 'n'
    • Ridley, A. J. & Hall, A. Snails, Swiss, and serum: the solution for Rac 'n' Rho. Cell 116, S23-S25 (2004).
    • (2004) Rho. Cell , vol.116
    • Ridley, A.J.1    Hall, A.2
  • 21
    • 0032577563 scopus 로고    scopus 로고
    • S. typhimurium Encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells
    • DOI 10.1016/S0092-8674(00)81442-7
    • Hardt, W. D., Chen, L. M., Schuebel, K. E., Bustelo, X. R. & Galan, J. E. S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 93, 815-826 (1998). (Pubitemid 28257587)
    • (1998) Cell , vol.93 , Issue.5 , pp. 815-826
    • Hardt, W.-D.1    Chen, L.-M.2    Schuebel, K.E.3    Bustelo, X.R.4    Galan, J.E.5
  • 23
    • 0041530031 scopus 로고    scopus 로고
    • A Burkholderia pseudomallei type III secreted protein, BopE, facilitates bacterial invasion of epithelial cells and exhibits guanine nucleotide exchange factor activity
    • DOI 10.1128/JB.185.16.4992-4996.2003
    • Stevens, M. P. et al. A Burkholderia pseudomallei type III secreted protein, BopE, facilitates bacterial invasion of epithelial cells and exhibits guanine nucleotide exchange factor activity. J. Bacteriol. 185, 4992-4996 (2003). (Pubitemid 36962307)
    • (2003) Journal of Bacteriology , vol.185 , Issue.16 , pp. 4992-4996
    • Stevens, M.P.1    Friebel, A.2    Taylor, L.A.3    Wood, M.W.4    Brown, P.J.5    Hardt, W.-D.6    Galyov, E.E.7
  • 24
    • 21244451603 scopus 로고    scopus 로고
    • IpgB1 is a novel Shigella effector protein involved in bacterial invasion of host cells: Its activity to promote membrane ruffling via Rac1 and Cdc42 activation
    • DOI 10.1074/jbc.M502509200
    • Ohya, K., Handa, Y., Ogawa, M., Suzuki, M. & Sasakawa, C. IpgB1 is a novel Shigella effector protein involved in bacterial invasion of host cells. Its activity to promote membrane ruffling via Rac1 and Cdc42 activation. J. Biol. Chem. 280, 24022-24034 (2005). (Pubitemid 40884890)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 24022-24034
    • Ohya, K.1    Handa, Y.2    Ogawa, M.3    Suzuki, M.4    Sasakawa, C.5
  • 26
    • 77952767396 scopus 로고    scopus 로고
    • Structure of Shigella IpgB2 in complex with human RhoA: Implications for the mechanism of bacterial guanine nucleotide exchange factor mimicry
    • Klink, B. U. et al. Structure of Shigella IpgB2 in complex with human RhoA: implications for the mechanism of bacterial guanine nucleotide exchange factor mimicry. J. Biol. Chem. 285, 17197-17208 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 17197-17208
    • Klink, B.U.1
  • 27
    • 77954295385 scopus 로고    scopus 로고
    • EspM2 is a RhoA guanine nucleotide exchange factor
    • Arbeloa, A. et al. EspM2 is a RhoA guanine nucleotide exchange factor. Cell. Microbiol. 12, 654-664 (2010).
    • (2010) Cell. Microbiol. , vol.12 , pp. 654-664
    • Arbeloa, A.1
  • 28
    • 58349102325 scopus 로고    scopus 로고
    • EspT triggers formation of lamellipodia and membrane ruffles through activation of Rac-1 and Cdc42
    • Bulgin, R. R., Arbeloa, A., Chung, J. C. & Frankel, G. EspT triggers formation of lamellipodia and membrane ruffles through activation of Rac-1 and Cdc42. Cell. Microbiol. 11, 217-229 (2009).
    • (2009) Cell. Microbiol. , vol.11 , pp. 217-229
    • Bulgin, R.R.1    Arbeloa, A.2    Chung, J.C.3    Frankel, G.4
  • 29
    • 55249084667 scopus 로고    scopus 로고
    • Structure and function of Salmonella SifA indicate that its interactions with SKIP SseJ, and RhoA family GTPases induce endosomal tubulation
    • Ohlson, M. B. et al. Structure and function of Salmonella SifA indicate that its interactions with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation. Cell Host Microbe 4, 434-446 (2008).
    • (2008) Cell Host Microbe , vol.4 , pp. 434-446
    • Ohlson, M.B.1
  • 30
    • 55249103138 scopus 로고    scopus 로고
    • Mimicry is the sincerest form of flattery?
    • Hume, P. J. & Koronakis, V. Mimicry is the sincerest form of flattery? Cell Host Microbe 4, 411-412 (2008).
    • (2008) Cell Host Microbe , vol.4 , pp. 411-412
    • Hume, P.J.1    Koronakis, V.2
  • 31
    • 84889234826 scopus 로고    scopus 로고
    • Targeting of Host Rab GTPase Function by the Intravacuolar Pathogen Legionella pneumophila
    • DOI 10.1016/j.devcel.2006.05.013, PII S1534580706002541
    • Machner, M. P. & Isberg, R. R. Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila. Dev. Cell 11, 47-56 (2006). (Pubitemid 43960806)
    • (2006) Developmental Cell , vol.11 , Issue.1 , pp. 47-56
    • Machner, M.P.1    Isberg, R.R.2
  • 33
    • 77949498580 scopus 로고    scopus 로고
    • Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA
    • Zhu, Y. et al. Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Proc. Natl Acad. Sci. USA 107, 4699-4704 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 4699-4704
    • Zhu, Y.1
  • 34
    • 72449132474 scopus 로고    scopus 로고
    • RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity
    • Schoebel, S., Oesterlin, L. K., Blankenfeldt, W., Goody, R. S. & Itzen, A. RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity. Mol. Cell 36, 1060-1072 (2009).
    • (2009) Mol. Cell , vol.36 , pp. 1060-1072
    • Schoebel, S.1    Oesterlin, L.K.2    Blankenfeldt, W.3    Goody, R.S.4    Itzen, A.5
  • 35
    • 78650973579 scopus 로고    scopus 로고
    • The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold
    • Selyunin, A. S. et al. The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold. Nature 469, 107-111 (2011).
    • (2011) Nature , vol.469 , pp. 107-111
    • Selyunin, A.S.1
  • 36
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • DOI 10.1126/science.1062023
    • Vetter, I. R. & Wittinghofer, A. The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304 (2001). (Pubitemid 33063089)
    • (2001) Science , vol.294 , Issue.5545 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 37
    • 0033575956 scopus 로고    scopus 로고
    • A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
    • Fu, Y. & Galan, J. E. A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 401, 293-297 (1999).
    • (1999) Nature , vol.401 , pp. 293-297
    • Fu, Y.1    Galan, J.E.2
  • 38
    • 0034097414 scopus 로고    scopus 로고
    • GAP activity of the Yersinia YopE cytotoxin specifically targets the Rho pathway: A mechanism for disruption of actin microfilament structure
    • DOI 10.1046/j.1365-2958.2000.01898.x
    • von Pawel-Rammingen, U. et al. GAP activity of the Yersinia YopE cytotoxin specifically targets the Rho pathway: a mechanism for disruption of actin microfilament structure. Mol. Microbiol. 36, 737-748 (2000). (Pubitemid 30258856)
    • (2000) Molecular Microbiology , vol.36 , Issue.3 , pp. 737-748
    • Von Pawel-Rammingen, U.1    Telepnev, M.V.2    Schmidt, G.3    Aktories, K.4    Wolf-Watz, H.5    Rosqvist, R.6
  • 39
    • 0033579479 scopus 로고    scopus 로고
    • The N-terminal domain of Pseudomonas aeruginosa exoenzyme S is a GTPase-activating protein for Rho GTPases
    • Goehring, U.-M., Schmidt, G., Pederson, K. J., Aktories, K. & Barbieri, J. T. The N-terminal domain of Pseudomonas aeruginosa exoenzyme S is a GTPase-activating protein for Rho GTPases. J. Biol. Chem. 274, 36369-36372 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 36369-36372
    • Goehring, U.-M.1    Schmidt, G.2    Pederson, K.J.3    Aktories, K.4    Barbieri, J.T.5
  • 40
    • 0033796738 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa ExoT is a Rho GTPase-activating protein
    • Krall, R., Schmidt, G., Aktories, K. & Barbieri, J. T. Pseudomonas aeruginosa ExoT is a Rho GTPase-activating protein. Infect. Immun. 68, 6066-6068 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 6066-6068
    • Krall, R.1    Schmidt, G.2    Aktories, K.3    Barbieri, J.T.4
  • 41
    • 53849133471 scopus 로고    scopus 로고
    • Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins
    • Deng, Q. & Barbieri, J. T. Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins. Annu. Rev. Microbiol. 62, 271-288 (2008).
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 271-288
    • Deng, Q.1    Barbieri, J.T.2
  • 42
    • 35348947419 scopus 로고    scopus 로고
    • Aeromonas exoenzyme T of Aeromonas salmonicida is a bifunctional protein that targets the host cytoskeleton
    • DOI 10.1074/jbc.M704797200
    • Fehr, D. et al. Aeromonas exoenzyme T of Aeromonas salmonicida is a bifunctional protein that targets the host cytoskeleton. J. Biol. Chem. 282, 28843-28852 (2007). (Pubitemid 47606029)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.39 , pp. 28843-28852
    • Fehr, D.1    Burr, S.E.2    Gibert, M.3    D'Alayer, J.4    Frey, J.5    Popoff, M.R.6
  • 43
    • 36249027095 scopus 로고    scopus 로고
    • Legionella pneumophila proteins that regulate Rab1 membrane cycling
    • DOI 10.1038/nature06336, PII NATURE06336
    • Ingmundson, A., Delprato, A., Lambright, D. G. & Roy, C. R. Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature 450, 365-369 (2007). (Pubitemid 350126758)
    • (2007) Nature , vol.450 , Issue.7168 , pp. 365-369
    • Ingmundson, A.1    Delprato, A.2    Lambright, D.G.3    Roy, C.R.4
  • 44
    • 0023110218 scopus 로고
    • Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from botulinum C2 toxin
    • DOI 10.1016/0014-5793(87)81566-1
    • Aktories, K., Weller, U. & Chhatwal, G. S. Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from botulinum C2 toxin. FEBS Lett. 212, 109-113 (1987). (Pubitemid 17028086)
    • (1987) FEBS Letters , vol.212 , Issue.1 , pp. 109-113
    • Aktories, K.1    Weller, U.2    Chhatwal, G.S.3
  • 45
    • 0023779031 scopus 로고
    • Functional modification of a 21-kilodalton G protein when ADP- ribosylated by exoenzyme C3 of Clostridium botulinum
    • Rubin, E. J., Gill, D. M., Boquet, P. & Popoff, M. R. Functional modification of a 21-kilodalton G protein when ADP- ribosylated by exoenzyme C3 of Clostridium botulinum. Mol. Cell. Biol. 8, 418-426 (1988).
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 418-426
    • Rubin, E.J.1    Gill, D.M.2    Boquet, P.3    Popoff, M.R.4
  • 46
    • 0024353843 scopus 로고
    • Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase
    • Sekine, A., Fujiwara, M. & Narumiya, S. Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. J. Biol. Chem. 264, 8602-8605 (1989). (Pubitemid 19151574)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.15 , pp. 8602-8605
    • Sekine, A.1    Fujiwara, M.2    Narumiya, S.3
  • 47
    • 33646905907 scopus 로고    scopus 로고
    • Localization of the C3-like ADP-ribosyltransferase from Staphylococcus aureus during bacterial invasion of mammalian cells
    • DOI 10.1128/IAI.02013-05
    • Molinari, G. et al. Localization of the C3-like ADP-ribosyltransferase from Staphylococcus aureus during bacterial invasion of mammalian cells. Infect. Immun. 74, 3673-3677 (2006). (Pubitemid 43794560)
    • (2006) Infection and Immunity , vol.74 , Issue.6 , pp. 3673-3677
    • Molinari, G.1    Rohde, M.2    Wilde, C.3    Just, I.4    Aktories, K.5    Chhatwal, G.S.6
  • 48
    • 77649216057 scopus 로고    scopus 로고
    • Selective and specific internalization of clostridial C3 ADP-ribosyltransferases into macrophages and monocytes
    • Fahrer, J. et al. Selective and specific internalization of clostridial C3 ADP-ribosyltransferases into macrophages and monocytes. Cell. Microbiol. 12, 233-247 (2010).
    • (2010) Cell. Microbiol. , vol.12 , pp. 233-247
    • Fahrer, J.1
  • 50
    • 0041707712 scopus 로고    scopus 로고
    • Entrapment of Rho ADP-ribosylated by Clostridium botulinum C3 exoenzyme in the Rho-guanine nucleotide dissociation inhibitor-1 complex
    • DOI 10.1074/jbc.M301915200
    • Genth, H. et al. Entrapment of Rho ADP-ribosylated by Clostridium botulinum C3 exoenzyme in the Rho-guanine nucleotide dissociation inhibitor-1 complex. J. Biol. Chem. 278, 28523-28527 (2003). (Pubitemid 36935755)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 28523-28527
    • Genth, H.1    Gerhard, R.2    Maeda, A.3    Amano, M.4    Kaibuchi, K.5    Aktories, K.6    Just, I.7
  • 51
    • 0032515914 scopus 로고    scopus 로고
    • Glucosylation and ADP ribosylation of Rho proteins: Effects on nucleotide binding, GTPase activity, and effector coupling
    • DOI 10.1021/bi972592c
    • Sehr, P. et al. Glucosylation and ADP-ribosylation of Rho proteins; effects on nucleotide binding, GTPase activity, and effector-coupling. Biochemistry 37, 5296-5304 (1998). (Pubitemid 28176531)
    • (1998) Biochemistry , vol.37 , Issue.15 , pp. 5296-5304
    • Sehr, P.1    Joseph, G.2    Genth, H.3    Just, I.4    Pick, E.5    Aktories, K.6
  • 52
    • 0025778012 scopus 로고
    • Alteration of the cytoskeleton of mammalian cells cultured in vitro by Clostridium botulinum C2 toxin and C3 ADP-ribosyltransferase
    • Wiegers, W. et al. Alteration of the cytoskeleton of mammalian cells cultured in vitro by Clostridium botulinum C2 toxin and C3 ADP- ribosyltransferase. Eur. J. Cell Biol. 54, 237-245 (1991).
    • (1991) Eur. J. Cell Biol. , vol.54 , pp. 237-245
    • Wiegers, W.1
  • 53
    • 33846814964 scopus 로고    scopus 로고
    • C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins
    • DOI 10.1007/s00210-006-0113-y
    • Vogelsgesang, M., Pautsch, A. & Aktories, K. C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins. Naunyn Schmiedebergs Arch. Pharmacol. 374, 347-360 (2007). (Pubitemid 46215285)
    • (2007) Naunyn-Schmiedeberg's Archives of Pharmacology , vol.374 , Issue.5-6 , pp. 347-360
    • Vogelsgesang, M.1    Pautsch, A.2    Aktories, K.3
  • 55
    • 77955302345 scopus 로고    scopus 로고
    • The Staphylococcus aureus epidermal cell differentiation inhibitor toxin promotes formation of infection foci in a mouse model of bacteremia
    • Munro, P. et al. The Staphylococcus aureus epidermal cell differentiation inhibitor toxin promotes formation of infection foci in a mouse model of bacteremia. Infect. Immun. 78, 3404-3411 (2010).
    • (2010) Infect. Immun. , vol.78 , pp. 3404-3411
    • Munro, P.1
  • 56
    • 27144457720 scopus 로고    scopus 로고
    • Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme
    • DOI 10.1038/sj.emboj.7600813, PII 7600813
    • Pautsch, A., Vogelsgesang, M., Trankle, J., Herrmann, C. & Aktories, K. Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme. EMBO J. 24, 3670-3680 (2005). (Pubitemid 41509373)
    • (2005) EMBO Journal , vol.24 , Issue.20 , pp. 3670-3680
    • Pautsch, A.1    Vogelsgesang, M.2    Trankle, J.3    Herrmann, C.4    Aktories, K.5
  • 57
    • 0030716497 scopus 로고    scopus 로고
    • Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue
    • DOI 10.1038/39651
    • Rittinger, K., Walker, P. A., Eccleston, J. F., Smerdon, S. J. & Gamblin, S. J. Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature 389, 758-762 (1997). (Pubitemid 27458966)
    • (1997) Nature , vol.389 , Issue.6652 , pp. 758-762
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Smerdon, S.J.4    Gamblin, S.J.5
  • 58
    • 0032127912 scopus 로고    scopus 로고
    • GTPase-activating proteins: Helping hands to complement an active site
    • DOI 10.1016/S0968-0004(98)01224-9, PII S0968000498012249
    • Scheffzek, K., Ahmadian, M. R. & Wittinghofer, A. GTPase-activating proteins: helping hands to complement an active site. Trends Biochem. Sci. 23, 257-262 (1998). (Pubitemid 28343370)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.7 , pp. 257-262
    • Scheffzek, K.1    Ahmadian, M.R.2    Wittinghofer, A.3
  • 59
    • 77649193972 scopus 로고    scopus 로고
    • Photorhabdus luminescens toxins ADP-ribosylate actin and RhoA to force actin clustering
    • Lang, A. E. et al. Photorhabdus luminescens toxins ADP-ribosylate actin and RhoA to force actin clustering. Science 327, 1139-1142 (2010).
    • (2010) Science , vol.327 , pp. 1139-1142
    • Lang, A.E.1
  • 60
    • 55249105923 scopus 로고    scopus 로고
    • Clostridium difficile - More difficult than ever
    • Kelly, C. P. & LaMont, J. T. Clostridium difficile - more difficult than ever. N. Engl. J. Med. 359, 1932-1940 (2008).
    • (2008) N. Engl. J. Med. , vol.359 , pp. 1932-1940
    • Kelly, C.P.1    Lamont, J.T.2
  • 61
    • 42149172381 scopus 로고    scopus 로고
    • Heterogeneity of large clostridial toxins: Importance of Clostridium difficile toxinotypes
    • DOI 10.1111/j.1574-6976.2008.00110.x
    • Rupnik, M. Heterogeneity of large clostridial toxins: importance of Clostridium difficile toxinotypes. FEMS Microbiol. Rev. 32, 541-555 (2008). (Pubitemid 351538749)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.3 , pp. 541-555
    • Rupnik, M.1
  • 62
    • 17444366186 scopus 로고    scopus 로고
    • Clostridium difficile toxins: Mechanism of action and role in disease
    • DOI 10.1128/CMR.18.2.247-263.2005
    • Voth, D. E. & Ballard, J. D. Clostridium difficile toxins: mechanism of action and role in disease. Clin. Microbiol. Rev. 18, 247-263 (2005). (Pubitemid 40548293)
    • (2005) Clinical Microbiology Reviews , vol.18 , Issue.2 , pp. 247-263
    • Voth, D.E.1    Ballard, J.D.2
  • 63
    • 0029054398 scopus 로고
    • Glucosylation of Rho proteins by Clostridium difficile toxin B
    • Just, I. et al. Glucosylation of Rho proteins by Clostridium difficile toxin B. Nature 375, 500-503 (1995).
    • (1995) Nature , vol.375 , pp. 500-503
    • Just, I.1
  • 65
    • 0029925007 scopus 로고    scopus 로고
    • Inactivation of Ras by Clostridium sordellii lethal toxin-catalyzed glucosylation
    • DOI 10.1074/jbc.271.17.10149
    • Just, I., Selzer, J., Hofmann, F., Green, G. A. & Aktories, K. Inactivation of Ras by Clostridium sordellii lethal toxin-catalyzed glucosylation. J. Biol. Chem. 271, 10149-10153 (1996). (Pubitemid 26131577)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.17 , pp. 10149-10153
    • Just, I.1    Selzer, J.2    Hofmann, F.3    Green, G.A.4    Aktories, K.5
  • 67
    • 79251471404 scopus 로고    scopus 로고
    • Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins
    • Nagahama, M. et al. Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins. Infect. Immun. 79, 905-910 (2011).
    • (2011) Infect. Immun. , vol.79 , pp. 905-910
    • Nagahama, M.1
  • 68
    • 0034283341 scopus 로고    scopus 로고
    • Structural consequences of mono-glucosylation of Ha-Ras by Clostridium sordellii lethal toxin
    • Vetter, I. R., Hofmann, F., Wohlgemuth, S., Herrmann, C. & Just, I. Structural consequences of mono-glucosylation of Ha-Ras by Clostridium sordellii lethal toxin. J. Mol. Biol. 301, 1091-1095 (2000).
    • (2000) J. Mol. Biol. , vol.301 , pp. 1091-1095
    • Vetter, I.R.1    Hofmann, F.2    Wohlgemuth, S.3    Herrmann, C.4    Just, I.5
  • 69
    • 0142135588 scopus 로고    scopus 로고
    • Glucosylation of Ras by Clostridium sordellii Lethal Toxin: Consequences for Effector Loop Conformations Observed by NMR Spectroscopy
    • DOI 10.1021/bi034529v
    • Geyer, M., Wilde, C., Selzer, J., Aktories, K. & Kalbitzer, H. R. Glucosylation of Ras by Clostridium sordellii lethal toxin: consequences for the effector loop conformations observed by NMR spectroscopy. Biochemistry 42, 11951-11959 (2003). (Pubitemid 37280645)
    • (2003) Biochemistry , vol.42 , Issue.41 , pp. 11951-11959
    • Geyer, M.1    Wilde, C.2    Selzer, J.3    Aktories, K.4    Kalbitzer, H.R.5
  • 70
    • 0032831781 scopus 로고    scopus 로고
    • Monoglucosylation of RhoA at Threonine-37 blocks cytosol-membrane cycling
    • Genth, H., Aktories, K. & Just, I. Monoglucosylation of RhoA at Threonine-37 blocks cytosol-membrane cycling. J. Biol. Chem. 274, 29050-29056 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 29050-29056
    • Genth, H.1    Aktories, K.2    Just, I.3
  • 72
    • 58149400542 scopus 로고    scopus 로고
    • AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling
    • Yarbrough, M. L. et al. AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science 323, 269-272 (2009).
    • (2009) Science , vol.323 , pp. 269-272
    • Yarbrough, M.L.1
  • 73
    • 67149136177 scopus 로고    scopus 로고
    • Fido a novel AMPylation domain common to fic, doc, and AvrB
    • Kinch, L. N., Yarbrough, M. L., Orth, K. & Grishin, N. V. Fido, a novel AMPylation domain common to fic, doc, and AvrB. PLoS ONE 4, e5818 (2009).
    • (2009) PLoS ONE , vol.4
    • Kinch, L.N.1    Yarbrough, M.L.2    Orth, K.3    Grishin, N.V.4
  • 74
    • 42949152423 scopus 로고    scopus 로고
    • Vibrio parahaemolyticus inhibition of Rho family GTPase activation requires a functional chromosome I type III secretion system
    • DOI 10.1128/IAI.01704-07
    • Casselli, T., Lynch, T., Southward, C. M., Jones, B. W. & DeVinney, R. Vibrio parahaemolyticus inhibition of Rho family GTPase activation requires a functional chromosome I type III secretion system. Infect. Immun. 76, 2202-2211 (2008). (Pubitemid 351656156)
    • (2008) Infection and Immunity , vol.76 , Issue.5 , pp. 2202-2211
    • Casselli, T.1    Lynch, T.2    Southward, C.M.3    Jones, B.W.4    DeVinney, R.5
  • 75
    • 63649139064 scopus 로고    scopus 로고
    • The Fic domain: Regulation of cell signaling by adenylylation
    • Worby, C. A. et al. The Fic domain: regulation of cell signaling by adenylylation. Mol. Cell 34, 93-103 (2009).
    • (2009) Mol. Cell , vol.34 , pp. 93-103
    • Worby, C.A.1
  • 78
    • 3142512687 scopus 로고    scopus 로고
    • Differentiate to thrive: Lessons from the Legionella pneumophila life cycle
    • DOI 10.1111/j.1365-2958.2004.04129.x
    • Molofsky, A. B. & Swanson, M. S. Differentiate to thrive: lessons from the Legionella pneumophila life cycle. Mol. Microbiol. 53, 29-40 (2004). (Pubitemid 38901377)
    • (2004) Molecular Microbiology , vol.53 , Issue.1 , pp. 29-40
    • Molofsky, A.B.1    Swanson, M.S.2
  • 79
    • 84889234796 scopus 로고    scopus 로고
    • A bifunctional bacterial protein links GDI displacement to Rab1 activation
    • DOI 10.1126/science.1149121
    • Machner, M. P. & Isberg, R. R. A bifunctional bacterial protein links GDI displacement to Rab1 activation. Science 318, 974-977 (2007). (Pubitemid 350098993)
    • (2007) Science , vol.318 , Issue.5852 , pp. 974-977
    • Machner, M.P.1    Isberg, R.R.2
  • 80
    • 64149084796 scopus 로고    scopus 로고
    • Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila
    • Brombacher, E. et al. Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila. J. Biol. Chem. 284, 4846-4856 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 4846-4856
    • Brombacher, E.1
  • 81
    • 77955872117 scopus 로고    scopus 로고
    • The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b
    • Muller, M. P. et al. The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science 329, 946-949 (2010).
    • (2010) Science , vol.329 , pp. 946-949
    • Muller, M.P.1
  • 82
    • 66149098151 scopus 로고    scopus 로고
    • Bacterial FIC proteins AMP up infection
    • Roy, C. R. & Mukherjee, S. Bacterial FIC proteins AMP up infection. Sci. Signal. 2, e14 (2009).
    • (2009) Sci. Signal. , vol.2
    • Roy, C.R.1    Mukherjee, S.2
  • 83
    • 0037205231 scopus 로고    scopus 로고
    • A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis
    • DOI 10.1016/S0092-8674(02)00766-3
    • Shao, F., Merritt, P. M., Bao, Z., Innes, R. W. & Dixon, J. E. A Yersinia effector and a Pseudomonas avirulence protein define a family of cycteine proteases functioning in bacterial pathogenesis. Cell 109, 575-588 (2002). (Pubitemid 34628721)
    • (2002) Cell , vol.109 , Issue.5 , pp. 575-588
    • Shao, F.1    Merritt, P.M.2    Bao, Z.3    Innes, R.W.4    Dixon, J.E.5
  • 85
    • 0035184874 scopus 로고    scopus 로고
    • Recombinant Yersinia YopT leads to uncoupling of RhoA-effector Interaction
    • DOI 10.1128/IAI.69.12.7535-7543.2001
    • Sorg, I., Goehring, U.-M., Aktories, K. & Schmidt, G. Recombinant Yersinia YopT leads to uncoupling of RhoA-effector interaction. Infect. Immun. 69, 7535-7543 (2001). (Pubitemid 33089239)
    • (2001) Infection and Immunity , vol.69 , Issue.12 , pp. 7535-7543
    • Sorg, I.1    Goehring, U.-M.2    Aktories, K.3    Schmidt, G.4
  • 87
    • 70350453627 scopus 로고    scopus 로고
    • Yersinia pseudotuberculosis virulence determinants invasin YopE, and YopT modulate RhoG activity and localization
    • Mohammadi, S. & Isberg, R. R. Yersinia pseudotuberculosis virulence determinants invasin, YopE, and YopT modulate RhoG activity and localization. Infect. Immun. 77, 4771-4782 (2009).
    • (2009) Infect. Immun. , vol.77 , pp. 4771-4782
    • Mohammadi, S.1    Isberg, R.R.2
  • 89
    • 0038485593 scopus 로고    scopus 로고
    • Novel mechanism of the co-regulation of nuclear transport of SmgGDS and Rac1
    • DOI 10.1074/jbc.M211286200
    • Lanning, C. C., Ruiz-Velasco, R. & Williams, C. L. Novel mechanism of the co-regulation of nuclear transport of SmgGDS and Rac1. J. Biol. Chem. 278, 12495-12506 (2003). (Pubitemid 36800238)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 12495-12506
    • Lanning, C.C.1    Ruiz-Velasco, R.2    Williams, C.L.3
  • 90
    • 6344231828 scopus 로고    scopus 로고
    • The Rac1 C-terminal polybasic region regulates the nuclear localization and protein degradation of Rac1
    • DOI 10.1074/jbc.M404977200
    • Lanning, C. C., Daddona, J. L., Ruiz-Velasco, R., Shafer, S. H. & Williams, C. L. The Rac1 C-terminal polybasic region regulates the nuclear localization and protein degradation of Rac1. J. Biol. Chem. 279, 44197-44210 (2004). (Pubitemid 39390727)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.42 , pp. 44197-44210
    • Lanning, C.C.1    Daddona, J.L.2    Ruiz-Velasco, R.3    Shafer, S.H.4    Williams, C.L.5
  • 91
    • 0034695446 scopus 로고    scopus 로고
    • CD44 interaction with Tiam1 promotes Rac1 signaling and hyaluronic acid- mediated breast tumor cell migration
    • DOI 10.1074/jbc.275.3.1829
    • Bourguignon, L. Y. W., Zhu, H., Shao, L. & Chen, Y. W. CD44 interaction with Tiam1 promotes Rac1 signaling and hyaluronic acid-mediated breast tumor cell migration. J. Biol. Chem. 275, 1829-1838 (2000). (Pubitemid 30060806)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.3 , pp. 1829-1838
    • Bourguignon, L.Y.W.1    Hongbo, Z.2    Shao, L.3    Chen, Y.W.4
  • 93
    • 67650115862 scopus 로고    scopus 로고
    • A family of bacterial cysteine protease type III effectors utilizes acylation-dependent and -independent strategies to localize to plasma membranes
    • Dowen, R. H., Engel, J. L., Shao, F., Ecker, J. R. & Dixon, J. E. A family of bacterial cysteine protease type III effectors utilizes acylation-dependent and -independent strategies to localize to plasma membranes. J. Biol. Chem. 284, 15867-15879 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 15867-15879
    • Dowen, R.H.1    Engel, J.L.2    Shao, F.3    Ecker, J.R.4    Dixon, J.E.5
  • 95
    • 0025707559 scopus 로고
    • A single protein of 110 kDa is associated with the multinucleating and necrotizing activity coded by the Vir plasmid of Escherichia coli
    • Oswald, E. & de Rycke, J. A single protein of 110 kDa is associated with the multinucleating and necrotizing activity coded by the Vir plasmid of Escherichia coli. FEMS Microbiol. Lett. 68, 279-284 (1990). (Pubitemid 20088764)
    • (1990) FEMS Microbiology Letters , vol.68 , Issue.3 , pp. 279-284
    • Oswald, E.1    De Rycke, J.2
  • 96
    • 68949145965 scopus 로고    scopus 로고
    • A new member of a growing toxin family - Escherichia coli cytotoxic necrotizing factor 3 (CNF3)
    • Stoll, T., Markwirth, G., Reipschlager, S. & Schmidt, G. A new member of a growing toxin family - Escherichia coli cytotoxic necrotizing factor 3 (CNF3). Toxicon 54, 745-753 (2009).
    • (2009) Toxicon , vol.54 , pp. 745-753
    • Stoll, T.1    Markwirth, G.2    Reipschlager, S.3    Schmidt, G.4
  • 97
    • 0036120223 scopus 로고    scopus 로고
    • Yersinia pseudotuberculosis produces a cytotoxic necrotizing factor
    • DOI 10.1128/IAI.70.5.2708-2714.2002
    • Lockman, H. A., Gillespie, R. A., Baker, B. D. & Shakhnovich, E. Yersinia pseudotuberculosis produces a cytotoxic necrotizing factor. Infect. Immun. 70, 2708-2714 (2002). (Pubitemid 34408421)
    • (2002) Infection and Immunity , vol.70 , Issue.5 , pp. 2708-2714
    • Lockman, H.A.1    Gillespie, R.A.2    Baker, B.D.3    Shakhnovich, E.4
  • 98
    • 0030742773 scopus 로고    scopus 로고
    • Molecular localization of the Escherichia coli cytotoxic necrotizing factor CNF1 cell-binding and catalytic domains
    • Lemichez, E., Flatau, G., Bruzzone, M., Boquet, P. & Gauthier, M. Molecular localization of the Escherichia coli cytotoxic necrotizing factor CNF1 cell-binding and catalytic domains. Mol. Microbiol. 24, 1061-1070 (1997). (Pubitemid 27286157)
    • (1997) Molecular Microbiology , vol.24 , Issue.5 , pp. 1061-1070
    • Lemichez, E.1    Flatau, G.2    Bruzzone, M.3    Boquet, P.4    Gauthier, M.5
  • 99
    • 12544255191 scopus 로고    scopus 로고
    • 67-kDa laminin receptor promotes internalization of cytotoxic necrotizing factor 1-expressing Escherichia coli K1 into human brain microvascular endothelial cells
    • Kim, K. J., Chung, J. W. & Kim, K. S. 67-kDa laminin receptor promotes internalization of cytotoxic necrotizing factor 1-expressing Escherichia coli K1 into human brain microvascular endothelial cells. J. Biol. Chem. 280, 1360-1368 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 1360-1368
    • Kim, K.J.1    Chung, J.W.2    Kim, K.S.3
  • 100
    • 34447253589 scopus 로고    scopus 로고
    • The cytotoxic necrotizing factors from Yersinia pseudotuberculosis and from Escherichia coli bind to different cellular receptors but take the same route to the cytosol
    • DOI 10.1128/IAI.01937-06
    • Blumenthal, B., Hoffmann, C., Aktories, K., Backert, S. & Schmidt, G. The cytotoxic necrotizing factors from Yersinia pseudotuberculosis and from Escherichia coli bind to different cellular receptors but take the same route to the cytosol. Infect. Immun. 75, 3344-3353 (2007). (Pubitemid 47040935)
    • (2007) Infection and Immunity , vol.75 , Issue.7 , pp. 3344-3353
    • Blumenthal, B.1    Hoffmann, C.2    Aktories, K.3    Backert, S.4    Schmidt, G.5
  • 101
    • 65449144434 scopus 로고    scopus 로고
    • Cleavage of Escherichia coli cytotoxic necrotizing factor 1 is required for full biologic activity
    • Knust, Z., Blumenthal, B., Aktories, K. & Schmidt, G. Cleavage of Escherichia coli cytotoxic necrotizing factor 1 is required for full biologic activity. Infect. Immun. 77, 1835-1841 (2009).
    • (2009) Infect. Immun. , vol.77 , pp. 1835-1841
    • Knust, Z.1    Blumenthal, B.2    Aktories, K.3    Schmidt, G.4
  • 102
    • 0030610785 scopus 로고    scopus 로고
    • Gin 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1
    • DOI 10.1038/42735
    • Schmidt, G. et al. Gln63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor 1. Nature 387, 725-729 (1997). (Pubitemid 27270615)
    • (1997) Nature , vol.387 , Issue.6634 , pp. 725-729
    • Schmidt, G.1    Sehr, P.2    Wilm, M.3    Selzer, J.4    Mann, M.5    Aktories, K.6
  • 104
    • 0034953089 scopus 로고    scopus 로고
    • Structure of the Rho-activating domain of Escherichia coli cytotoxic necrotizing factor 1
    • DOI 10.1038/89610
    • Buetow, L., Flatau, G., Chiu, K., Boquet, P. & Ghosh, P. Structure of the Rho-activating domain of Escherichia coli cytotoxic necrotizing factor 1. Nature Struct. Biol. 8, 584-588 (2001). (Pubitemid 32613004)
    • (2001) Nature Structural Biology , vol.8 , Issue.7 , pp. 584-588
    • Buetow, L.1    Flatau, G.2    Chiu, K.3    Boquet, P.4    Ghosh, P.5
  • 105
    • 0032867338 scopus 로고    scopus 로고
    • Identification of the region of Rho involved in substrate recognition by Escherichia coli cytotoxic necrotizing factor 1 (CNF1)
    • Lerm, M., Schmidt, G., Goehring, U.-M., Schirmer, J. & Aktories, K. Identification of the region of Rho involved in substrate recognition by Escherichia coli cytotoxic necrotizing factor 1 (CNF1). J. Biol. Chem. 274, 28999-29004 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 28999-29004
    • Lerm, M.1    Schmidt, G.2    Goehring, U.-M.3    Schirmer, J.4    Aktories, K.5
  • 106
    • 17444434479 scopus 로고
    • Interaction of Escherichia coli cytotoxic necrotizing factor type 1 (CNF1) with cultured cells
    • Falzano, L., Fiorentini, C., Boquet, P. & Donelli, G. Interaction of Escherichia coli cytotoxic necrotizing factor type 1 (CNF1) with cultured cells. Cytotechnology 11, S56-S58 (1993).
    • (1993) Cytotechnology , vol.11
    • Falzano, L.1    Fiorentini, C.2    Boquet, P.3    Donelli, G.4
  • 107
    • 0024638664 scopus 로고
    • Cytotoxic effect of multinucleation in HeLa cell cultures associated with the presence of Vir plasmid in Escherichia coli strains
    • Oswald, E., de Rycke, J., Guillot, J. F. & Boivin, R. Cytotoxic effect of multinucleation in HeLa cell cultures associated with the presence of Vir plasmid in Escherichia coli strains. FEMS Microbiol. Lett. 58, 95-100 (1989).
    • (1989) FEMS Microbiol. Lett. , vol.58 , pp. 95-100
    • Oswald, E.1    De Rycke, J.2    Guillot, J.F.3    Boivin, R.4
  • 108
    • 0031563151 scopus 로고    scopus 로고
    • Uncoupling of S-phase and mitosis by recombinant cytotoxic necrotizing factor 2 (CNF2)
    • DOI 10.1006/excr.1997.3595
    • Denko, N., Langland, R., Barton, M. & Lieberman, M. A. Uncoupling of S-phase and mitosis by recombinant cytotoxic necrotizing factor 2 (CNF2). Exp. Cell Res. 234, 132-138 (1997). (Pubitemid 27317910)
    • (1997) Experimental Cell Research , vol.234 , Issue.1 , pp. 132-138
    • Denko, N.1    Langland, R.2    Barton, M.3    Lieberman, M.A.4
  • 109
    • 33646268174 scopus 로고    scopus 로고
    • Is the Rac GTPase-activating toxin CNF1 a smart hijacker of host cell fate?
    • DOI 10.1096/fj.05-4706hyp
    • Malorni, W. & Fiorentini, C. Is the Rac GTPase-activating toxin CNF1 a smart hijacker of host cell fate? FASEB J. 20, 606-609 (2006). (Pubitemid 44933304)
    • (2006) FASEB Journal , vol.20 , Issue.6 , pp. 606-609
    • Malorni, W.1    Fiorentini, C.2
  • 111
    • 0036070562 scopus 로고    scopus 로고
    • Proteasomal degradation of cytotoxic necrotizing factor 1-activated Rac
    • DOI 10.1128/IAI.70.8.4053-4058.2002
    • Lerm, M., Pop, M., Fritz, G., Aktories, K. & Schmidt, G. Proteasomal degradation of cytotoxic necrotizing factor 1-activated Rac. Infect. Immun. 70, 4053-4058 (2002). (Pubitemid 34790912)
    • (2002) Infection and Immunity , vol.70 , Issue.8 , pp. 4053-4058
    • Lerm, M.1    Pop, M.2    Fritz, G.3    Aktories, K.4    Schmidt, G.5
  • 115
    • 0024335143 scopus 로고
    • Purification and characterization of Bordetella bronchiseptica dermonecrotic toxin
    • DOI 10.1016/0882-4010(89)90078-8
    • Horiguchi, Y., Nakai, T. & Kume, K. Purification and characterization of Bordetella bronchiseptica dermonecrotic toxin. Microb. Pathogen. 6, 361-368 (1989). (Pubitemid 19182108)
    • (1989) Microbial Pathogenesis , vol.6 , Issue.5 , pp. 361-368
    • Horiguchi, Y.1    Nakai, T.2    Kume, K.3
  • 116
    • 79951990525 scopus 로고    scopus 로고
    • Bordetella dermonecrotic toxin binds to target cells via the N-terminal 30 amino acids
    • Fukui-Miyazaki, A., Ohnishi, S., Kamitani, S., Abe, H. & Horiguchi, Y. Bordetella dermonecrotic toxin binds to target cells via the N-terminal 30 amino acids. Microbiol. Immunol. 55, 154-159 (2011).
    • (2011) Microbiol. Immunol. , vol.55 , pp. 154-159
    • Fukui-Miyazaki, A.1    Ohnishi, S.2    Kamitani, S.3    Abe, H.4    Horiguchi, Y.5
  • 117
    • 1642453672 scopus 로고    scopus 로고
    • Bordetella Dermonecrotic Toxin Undergoes Proteolytic Processing to Be Translocated from a Dynamin-related Endosome into the Cytoplasm in an Acidification-independent Manner
    • DOI 10.1074/jbc.M310340200
    • Matsuzawa, T. et al. Bordetella dermonecrotic toxin undergoes proteolytic processing to be translocated from a dynamin-related endosome into the cytoplasma in an acidification-independent manner. J. Biol. Chem. 279, 2866-2872 (2004). (Pubitemid 38114278)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.4 , pp. 2866-2872
    • Matsuzawa, T.1    Fukui, A.2    Kashimoto, T.3    Nagao, K.4    Oka, K.5    Miyake, M.6    Horiguchi, Y.7
  • 118
    • 0033527746 scopus 로고    scopus 로고
    • Identification of the C-terminal part of Bordetella dermonecrotic toxin as a transglutaminase for Rho GTPases
    • Schmidt, G., Goehring, U.-M., Schirmer, J., Lerm, M. & Aktories, K. Identification of the C-terminal part of Bordetella dermonecrotic toxin as a transglutaminase for Rho GTPases. J. Biol. Chem. 274, 31875-31881 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 31875-31881
    • Schmidt, G.1    Goehring, U.-M.2    Schirmer, J.3    Lerm, M.4    Aktories, K.5
  • 120
    • 0032577588 scopus 로고    scopus 로고
    • The Rho-deamidating cytotoxic necrotizing factor 1 from Escherichia coli possesses transglutaminase activity: Cysteine 866 and histidine 881 are essential for enzyme activity
    • DOI 10.1074/jbc.273.22.13669
    • Schmidt, G., Selzer, J., Lerm, M. & Aktories, K. The Rho-deamidating cytotoxic-necrotizing factor CNF1 from Escherichia coli possesses transglutaminase activity. Cysteine-866 and histidine-881 are essential for enzyme activity. J. Biol. Chem. 273, 13669-13674 (1998). (Pubitemid 28268413)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.22 , pp. 13669-13674
    • Schmidt, G.1    Selzer, J.2    Lerm, M.3    Aktories, K.4
  • 121
    • 0347349553 scopus 로고
    • Mechanism of cholera toxin action: Covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system
    • Cassel, D. & Pfeuffer, T. Mechanism of cholera toxin action: covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system. Proc. Natl Acad. Sci. USA 75, 2669-2673 (1978). (Pubitemid 8375048)
    • (1978) Proceedings of the National Academy of Sciences of the United States of America , vol.75 , Issue.6 , pp. 2669-2673
    • Cassel, D.1    Pfeuffer, T.2
  • 123
    • 66349099617 scopus 로고    scopus 로고
    • Pasteurella multocida toxin activation of heterotrimeric G proteins by deamidation
    • Orth, J. H. et al. Pasteurella multocida toxin activation of heterotrimeric G proteins by deamidation. Proc. Natl Acad. Sci. USA 106, 7179-7184 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 7179-7184
    • Orth, J.H.1
  • 124
    • 33646948992 scopus 로고    scopus 로고
    • New insights into the role of conserved, essential residues in the GTP binding/GTP hydrolytic cycle of large G proteins
    • DOI 10.1074/jbc.M513837200
    • Majumdar, S., Ramachandran, S. & Cerione, R. A. New insights into the role of conserved, essential residues in the GTP binding/GTP hydrolytic cycle of large G proteins. J. Biol. Chem. 281, 9219-9226 (2006). (Pubitemid 43864637)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9219-9226
    • Majumdar, S.1    Ramachandran, S.2    Cerione, R.A.3
  • 125
    • 0027965652 scopus 로고
    • Structures of active conformations of Giα1 and the mechanism of GTP hydrolysis
    • Coleman, D. E. et al. Structures of active conformations of Giα1 and the mechanism of GTP hydrolysis. Science 265, 1405-1412 (1994).
    • (1994) Science , vol.265 , pp. 1405-1412
    • Coleman, D.E.1
  • 126
    • 0021321632 scopus 로고
    • Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin
    • Van Dop, C., Tsubokawa, M., Bourne, H. R. & Ramachandran, J. Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin. J. Biol. Chem. 259, 696-698 (1984). (Pubitemid 14192128)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.2 , pp. 696-698
    • Van Dop, C.1    Tsubokawa, M.2    Bourne, H.R.3    Ramachandran, J.4
  • 127
    • 0024854388 scopus 로고
    • 187 results in loss of GTPase activity
    • Freissmuth, M. & Gilman, A. G. Mutations of GSα designed to alter the reactivity of the protein with bacterial toxins. Substitutions at ARG187 result in loss of GTPase activity. J. Biol. Chem. 264, 21907-21914 (1989). (Pubitemid 20028767)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.36 , pp. 21907-21914
    • Freissmuth, M.1    Gilman, A.G.2
  • 128
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • DOI 10.1146/annurev.biochem.66.1.639
    • Sprang, S. R. G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66, 639-678 (1997). (Pubitemid 27274670)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 129
    • 0031012747 scopus 로고    scopus 로고
    • Pasteurella multocida toxin activates the inositol triphosphate signaling pathway in Xenopus oocytes via G(q)α-coupled phospholipase C-β1
    • DOI 10.1074/jbc.272.2.1268
    • Wilson, B. A., Zhu, X., Ho, M. & Lu, L. Pasteurella multocida toxin activates the inositol triphosphate signaling pathway in Xenopus oocytes via Gqα-coupled phospholipase C-β1. J. Biol. Chem. 272, 1268-1275 (1997). (Pubitemid 27034627)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.2 , pp. 1268-1275
    • Wilson, B.A.1    Zhu, X.2    Ho, M.3    Lu, L.4
  • 130
    • 34047276113 scopus 로고    scopus 로고
    • Modulation of host cell gene expression through activation of STAT transcription factors by Pasteurella multocida toxin
    • DOI 10.1074/jbc.M609018200
    • Orth, J. H., Aktories, K. & Kubatzky, K. F. Modulation of host cell gene expression through activation of STAT transcription factors by Pasteurella multocida toxin. J. Biol. Chem. 282, 3050-3057 (2007). (Pubitemid 47084349)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.5 , pp. 3050-3057
    • Orth, J.H.C.1    Aktories, K.2    Kubatzky, K.F.3
  • 131
    • 59749099895 scopus 로고    scopus 로고
    • Pasteurella multocida toxin activates Gβγ dimers of heterotrimeric G proteins
    • Preuss, I., Kurig, B., N?rnberg, B., Orth, J. H. & Aktories, K. Pasteurella multocida toxin activates Gβγ dimers of heterotrimeric G proteins. Cell. Signal. 21, 551-558 (2009).
    • (2009) Cell. Signal. , vol.21 , pp. 551-558
    • Preuss, I.1    Kurig, B.2    Nrnberg, B.3    Orth, J.H.4    Aktories, K.5
  • 132
    • 77957127483 scopus 로고    scopus 로고
    • Pasteurella multocida toxin is a potent activator of anti-apoptotic signalling pathways
    • Preuss, I., Hildebrand, D., Orth, J. H., Aktories, K. & Kubatzky, K. F. Pasteurella multocida toxin is a potent activator of anti-apoptotic signalling pathways. Cell. Microbiol. 12, 1174-1185 (2010).
    • (2010) Cell. Microbiol. , vol.12 , pp. 1174-1185
    • Preuss, I.1    Hildebrand, D.2    Orth, J.H.3    Aktories, K.4    Kubatzky, K.F.5
  • 133
    • 27744535465 scopus 로고    scopus 로고
    • 12/13
    • DOI 10.1074/jbc.M507203200
    • Orth, J. H., Lang, S., Taniguchi, M. & Aktories, K. Pasteurella multocida toxin-induced activation of RhoA is mediated via two families of Gα proteins, Gαq and Gα12/13. J. Biol. Chem. 280, 36701-36707 (2005). (Pubitemid 41587748)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.44 , pp. 36701-36707
    • Orth, J.H.C.1    Lang, S.2    Taniguchi, M.3    Aktories, K.4
  • 136
    • 0035830825 scopus 로고    scopus 로고
    • Pleiotropic effects of Pasteurella multocida toxin are mediated by Gq-dependent and -independent mechanisms Involvement of Gq but not G11
    • Zywietz, A., Gohla, A., Schmelz, M., Schultz, G. & Offermanns, S. Pleiotropic effects of Pasteurella multocida toxin are mediated by Gq-dependent and -independent mechanisms. Involvement of Gq but not G11. J. Biol. Chem. 276, 3840-3845 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 3840-3845
    • Zywietz, A.1    Gohla, A.2    Schmelz, M.3    Schultz, G.4    Offermanns, S.5
  • 137
    • 0030891386 scopus 로고    scopus 로고
    • Localization of the glucosyltransferase activity of Clostridium difficile toxin B to the N-terminal part of the holotoxin
    • DOI 10.1074/jbc.272.17.11074
    • Hofmann, F., Busch, C., Prepens, U., Just, I. & Aktories, K. Localization of the glucosyltransferase activity of Clostridium difficile toxin B to the N-terminal part of the holotoxin. J. Biol. Chem. 272, 11074-11078 (1997). (Pubitemid 27184097)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.17 , pp. 11074-11078
    • Hofmann, F.1    Busch, C.2    Prepens, U.3    Just, I.4    Aktories, K.5
  • 139
    • 34548472183 scopus 로고    scopus 로고
    • Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity
    • DOI 10.1074/jbc.M703062200
    • Egerer, M., Giesemann, T., Jank, T., Satchell, K. J. & Aktories, K. Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on a cysteine protease activity. J. Biol. Chem. 282, 25314-25321 (2007). (Pubitemid 47372781)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.35 , pp. 25314-25321
    • Egerer, M.1    Giesemann, T.2    Jank, T.3    Satchell, K.J.4    Aktories, K.5
  • 140
    • 79952418425 scopus 로고    scopus 로고
    • Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B
    • Genisyuerek, S. et al. Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B. Mol. Microbiol. 79, 1643-1654 (2011).
    • (2011) Mol. Microbiol. , vol.79 , pp. 1643-1654
    • Genisyuerek, S.1
  • 142
    • 0242414631 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium difficile toxin B. Translocation of the N-terminal catalytic domain into the cytosol of eukaryotic cells
    • DOI 10.1074/jbc.M307540200
    • Pfeifer, G. et al. Cellular uptake of Clostridium difficile toxin B: translocation of the N-terminal catalytic domain into the cytosol of eukaryotic cells. J. Biol. Chem. 278, 44535-44541 (2003). (Pubitemid 37377206)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 44535-44541
    • Pfeifer, G.1    Schirmer, J.2    Leemhuis, J.3    Busch, C.4    Meyer, D.K.5    Aktories, K.6    Barth, H.7
  • 143
    • 77955782233 scopus 로고    scopus 로고
    • Structural organization of the functional domains of Clostridium difficile toxins A and B
    • Pruitt, R. N., Chambers, M. G., Ng, K. K., Ohi, M. D. & Lacy, D. B. Structural organization of the functional domains of Clostridium difficile toxins A and B. Proc. Natl Acad. Sci. USA 107, 13467-13472 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 13467-13472
    • Pruitt, R.N.1    Chambers, M.G.2    Ng, K.K.3    Ohi, M.D.4    Lacy, D.B.5
  • 144
    • 30444435782 scopus 로고    scopus 로고
    • Heterotrimeric G-proteins: A short history
    • DOI 10.1038/sj.bjp.0706405, PII 0706405
    • Milligan, G. & Kostenis, E. Heterotrimeric G-proteins: a short history. Br. J. Pharmacol. 147, S46-S55 (2006). (Pubitemid 43077261)
    • (2006) British Journal of Pharmacology , vol.147 , Issue.SUPPL. 1
    • Milligan, G.1    Kostenis, E.2
  • 146
    • 42449139551 scopus 로고    scopus 로고
    • The guanine-nucleotide-exchange factor BopE from Burkholderia pseudomallei adopts a compact version of the Salmonella SopE/SopE2 fold and undergoes a closed-to-open conformational change upon interaction with Cdc42
    • DOI 10.1042/BJ20071546
    • Upadhyay, A. et al. The guanine-nucleotide-exchange factor BopE from Burkholderia pseudomallei adopts a compact version of the Salmonella SopE/SopE2 fold and undergoes a closed-to-open conformational change upon interaction with Cdc42. Biochem. J. 411, 485-493 (2008). (Pubitemid 351600733)
    • (2008) Biochemical Journal , vol.411 , Issue.3 , pp. 485-493
    • Upadhyay, A.1    Wu, H.-L.2    Williams, C.3    Field, T.4    Galyov, E.E.5    Van Den Elsen, J.M.H.6    Bagby, S.7
  • 147
    • 68249146082 scopus 로고    scopus 로고
    • Structural insights into host GTPase isoform selection by a family of bacterial GEF mimics
    • Huang, Z. et al. Structural insights into host GTPase isoform selection by a family of bacterial GEF mimics. Nature Struct. Mol. Biol. 16, 853-860 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 853-860
    • Huang, Z.1
  • 150
    • 0034685024 scopus 로고    scopus 로고
    • Deamidation of RhoA glutamine 63 by the Escherichia coli CNF1 toxin requires a short sequence of the GTPase switch 2 domain
    • DOI 10.1006/bbrc.1999.1904
    • Flatau, G., Landraud, L., Boquet, P., Bruzzone, M. & Munro, P. Deamidation of RhoA glutamine 63 by the Escherichia coli CNF1 toxin requires a short sequence of the GTPase switch 2 domain. Biochem. Biophys. Res. Commun. 267, 588-592 (2000). (Pubitemid 30076842)
    • (2000) Biochemical and Biophysical Research Communications , vol.267 , Issue.2 , pp. 588-592
    • Flatau, G.1    Landraud, L.2    Boquet, P.3    Bruzzone, M.4    Munro, P.5
  • 151
    • 0030611230 scopus 로고    scopus 로고
    • Bordetella bronchiseptica dermonecrotizing toxin induces reorganization of actin stress fibers through deamidation of Gln-63 of the GTP-binding protein Rho
    • Horiguchi, Y. et al. Bordetella bronchiseptica dermonecrotizing toxin induces reorganization of actin stress fibers through deamidation of Gln-63 of the GTP-binding protein Rho. Proc. Natl Acad. Sci. USA 94, 11623-11626 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11623-11626
    • Horiguchi, Y.1
  • 152
    • 0026524741 scopus 로고
    • ADP-ribosylation of signal-transducing guanine nucleotide-binding proteins by pertussis toxin
    • Gierschik, P. ADP-ribosylation of signal-transducing guanine nucleotide-binding proteins by pertussis toxin. Curr. Top. Microbiol. Immunol. 175, 69-98 (1992).
    • (1992) Curr. Top. Microbiol. Immunol. , vol.175 , pp. 69-98
    • Gierschik, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.