메뉴 건너뛰기




Volumn 4, Issue 180, 2011, Pages

Bacterial scaffolds assemble novel higher-order complexes to reengineer eukaryotic cell processes

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROQUINE; GLUCOCORTICOID; GLUCOCORTICOID RECEPTOR; BACTERIAL PROTEIN;

EID: 79960103788     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2002252     Document Type: Review
Times cited : (1)

References (32)
  • 1
    • 0033575956 scopus 로고    scopus 로고
    • A salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
    • Y. Fu, J. E. Galán, 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    Galán, J.E.2
  • 2
    • 0032577563 scopus 로고    scopus 로고
    • S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffl ing and nuclear responses in host cells
    • W. D. Hardt, L. M. Chen, K. E. Schuebel, X. R. Bustelo, J. E. Galán, S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffl ing and nuclear responses in host cells. Cell 93, 815-826 (1998).
    • (1998) Cell , vol.93 , pp. 815-826
    • Hardt, W.D.1    Chen, L.M.2    Schuebel, K.E.3    Bustelo, X.R.4    Galán, J.E.5
  • 4
    • 33847154642 scopus 로고    scopus 로고
    • The phosphothreonine lyase activity of a bacterial type III effector family
    • H. Li, H. Xu, Y. Zhou, J. Zhang, C. Long, S. Li, S. Chen, J. M. Zhou, F. Shao, The phosphothreonine lyase activity of a bacterial type III effector family. Science 315, 1000-1003 (2007).
    • (2007) Science , vol.315 , pp. 1000-1003
    • Li, H.1    Xu, H.2    Zhou, Y.3    Zhang, J.4    Long, C.5    Li, S.6    Chen, S.7    Zhou, J.M.8    Shao, F.9
  • 5
    • 33744457909 scopus 로고    scopus 로고
    • Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation
    • S. Mukherjee, G. Keitany, Y. Li, Y. Wang, H. L. Ball, E. J. Goldsmith, K. Orth, Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation. Science 312, 1211-1214 (2006).
    • (2006) Science , vol.312 , pp. 1211-1214
    • Mukherjee, S.1    Keitany, G.2    Li, Y.3    Wang, Y.4    Ball, H.L.5    Goldsmith, E.J.6    Orth, K.7
  • 7
    • 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
    • M. B. Ohlson, Z. Huang, N. M. Alto, M. P. Blanc, J. E. Dixon, J. Chai, S. I. Miller, 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    Huang, Z.2    Alto, N.M.3    Blanc, M.P.4    Dixon, J.E.5    Chai, J.6    Miller, S.I.7
  • 9
    • 0035024818 scopus 로고    scopus 로고
    • EspG, a novel type III system-secreted protein from enteropathogenic Escherichia coli with similarities to VirA of Shigella fl exneri
    • S. J. Elliott, E. O. Krejany, J. L. Mellies, R. M. Robins- Browne, C. Sasakawa, J. B. Kaper, EspG, a novel type III system-secreted protein from enteropathogenic Escherichia coli with similarities to VirA of Shigella fl exneri. Infect. Immun. 69, 4027-4033 (2001).
    • (2001) Infect. Immun. , vol.69 , pp. 4027-4033
    • Elliott, S.J.1    Krejany, E.O.2    Mellies, J.L.3    Robins- Browne, R.M.4    Sasakawa, C.5    Kaper, J.B.6
  • 12
    • 33845432262 scopus 로고    scopus 로고
    • Aquaporins contribute to diarrhoea caused by attaching and effacing bacterial pathogens
    • J. A. Guttman, F. N. Samji, Y. Li, W. Deng, A. Lin, B. B. Finlay, Aquaporins contribute to diarrhoea caused by attaching and effacing bacterial pathogens. Cell. Microbiol. 9, 131-141 (2007).
    • (2007) Cell. Microbiol. , vol.9 , pp. 131-141
    • Guttman, J.A.1    Samji, F.N.2    Li, Y.3    Deng, W.4    Lin, A.5    Finlay, B.B.6
  • 13
    • 0038554077 scopus 로고    scopus 로고
    • Biology of the p21-activated kinases
    • G. M. Bokoch, Biology of the p21-activated kinases. Annu. Rev. Biochem. 72, 743-781 (2003).
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 743-781
    • Bokoch, G.M.1
  • 14
  • 15
    • 0034604338 scopus 로고    scopus 로고
    • Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    • M. Lei, W. Lu, W. Meng, M. C. Parrini, M. J. Eck, B. J. Mayer, S. C. Harrison, Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell 102, 387-397 (2000).
    • (2000) Cell , vol.102 , pp. 387-397
    • Lei, M.1    Lu, W.2    Meng, W.3    Parrini, M.C.4    Eck, M.J.5    Mayer, B.J.6    Harrison, S.C.7
  • 16
    • 79851474020 scopus 로고    scopus 로고
    • Structural and functional studies indicate that the EPEC effector, EspG, directly binds p21-activated kinase
    • K. L. Germane, B. W. Spiller, Structural and functional studies indicate that the EPEC effector, EspG, directly binds p21-activated kinase. Biochemistry 50, 917-919 (2011).
    • (2011) Biochemistry , vol.50 , pp. 917-919
    • Germane, K.L.1    Spiller, B.W.2
  • 17
    • 0033574449 scopus 로고    scopus 로고
    • The advantage of being uncompetitive
    • P. Chardin, F. McCormick, Brefeldin A: The advantage of being uncompetitive. Cell 97, 153-155 (1999).
    • (1999) Cell , vol.97 , pp. 153-155
    • Chardin, P.1    McCormick, F.2    Brefeldin, A.3
  • 20
    • 0036120245 scopus 로고    scopus 로고
    • A gene from the locus of enterocyte effacement that is required for enteropathogenic Escherichia coli to increase tight-junction permeability encodes a chaperone for EspF
    • S. J. Elliott, C. B. O'Connell, A. Koutsouris, C. Brinkley, M. S. Donnenberg, G. Hecht, J. B. Kaper, A gene from the locus of enterocyte effacement that is required for enteropathogenic Escherichia coli to increase tight-junction permeability encodes a chaperone for EspF. Infect. Immun. 70, 2271-2277 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 2271-2277
    • Elliott, S.J.1    O'Connell, C.B.2    Koutsouris, A.3    Brinkley, C.4    Donnenberg, M.S.5    Hecht, G.6    Kaper, J.B.7
  • 21
    • 33746928447 scopus 로고    scopus 로고
    • Characterization of TccP-mediated N-WASP activation during enterohaemorrhagic Escherichia coli infection
    • J. Garmendia, M. F. Carlier, C. Egile, D. Didry, G. Frankel, Characterization of TccP-mediated N-WASP activation during enterohaemorrhagic Escherichia coli infection. Cell. Microbiol. 8, 1444-1455 (2006).
    • (2006) Cell. Microbiol. , vol.8 , pp. 1444-1455
    • Garmendia, J.1    Carlier, M.F.2    Egile, C.3    Didry, D.4    Frankel, G.5
  • 22
    • 4344656777 scopus 로고    scopus 로고
    • U is a translocated EHEC effector that interacts with Tir and N-WASP and promotes Nck-independent actin assembly
    • U is a translocated EHEC effector that interacts with Tir and N-WASP and promotes Nck-independent actin assembly. Dev. Cell 7, 217-228 (2004).
    • (2004) Dev. Cell , vol.7 , pp. 217-228
    • Campellone, K.G.1    Robbins, D.2    Leong, J.M.3
  • 23
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • R. Rohatgi, L. Ma, H. Miki, M. Lopez, T. Kirchhausen, T. Takenawa, M. W. Kirschner, The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97, 221-231 (1999).
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5    Takenawa, T.6    Kirschner, M.W.7
  • 24
    • 0344443719 scopus 로고    scopus 로고
    • Sorting nexin 9 participates in clathrin-mediated endocytosis through interactions with the core components
    • R. Lundmark, S. R. Carlsson, Sorting nexin 9 participates in clathrin-mediated endocytosis through interactions with the core components. J. Biol. Chem. 278, 46772-46781 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 46772-46781
    • Lundmark, R.1    Carlsson, S.R.2
  • 25
    • 34249722773 scopus 로고    scopus 로고
    • Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with distinct fi lament bundling properties
    • T. H. Millard, J. Dawson, L. M. Machesky, Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with distinct fi lament bundling properties. J. Cell Sci. 120, 1663-1672 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 1663-1672
    • Millard, T.H.1    Dawson, J.2    Machesky, L.M.3
  • 28
    • 25444476973 scopus 로고    scopus 로고
    • SseJ deacylase activity by Salmonella enterica serovar Typhimurium promotes virulence in mice
    • M. B. Ohlson, K. Fluhr, C. L. Birmingham, J. H. Brumell, S. I. Miller, SseJ deacylase activity by Salmonella enterica serovar Typhimurium promotes virulence in mice. Infect. Immun. 73, 6249-6259 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 6249-6259
    • Ohlson, M.B.1    Fluhr, K.2    Birmingham, C.L.3    Brumell, J.H.4    Miller, S.I.5
  • 31
    • 18844406751 scopus 로고    scopus 로고
    • The intracellular fate of Salmonella depends on the recruitment of kinesin
    • E. Boucrot, T. Henry, J. P. Borg, J. P. Gorvel, S. Méresse, The intracellular fate of Salmonella depends on the recruitment of kinesin. Science 308, 1174-1178 (2005).
    • (2005) Science , vol.308 , pp. 1174-1178
    • Boucrot, E.1    Henry, T.2    Borg, J.P.3    Gorvel, J.P.4    Méresse, S.5
  • 32
    • 79960093663 scopus 로고    scopus 로고
    • note
    • Funding: This work was supported by NIH R01 64285 to C.F.L. and NIH R01 AI46454 to J.M.L.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.