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Volumn 3, Issue 4, 2011, Pages 356-368

Cycle inhibiting factors (Cifs): Cyclomodulins that usurp the ubiquitin-dependent degradation pathway of host cells

Author keywords

Bacterial toxin; Cullin RING E3 ubiquitin ligase; Eukaryotic cell cycle; NEDD8; Type III secretion system; Ubiquitin

Indexed keywords

ACTIN; BACTERIAL PROTEIN; CULLIN RING UBIQUITIN LIGASE; CYCLE INHIBITING FACTOR; CYCLOMODULIN; NEDD8 PROTEIN; PROTEASOME; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 79955610450     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins3040356     Document Type: Review
Times cited : (39)

References (52)
  • 1
    • 0031004990 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli O103 from rabbit elicits actin stress fibers and focal adhesions in HeLa epithelial cells, cytopathic effects that are linked to an analog of the locus of enterocyte effacement
    • de Rycke, J.; Comtet, E.; Chalareng, C.; Boury, M.; Tasca, C.; Milon, A. Enteropathogenic Escherichia coli O103 from rabbit elicits actin stress fibers and focal adhesions in HeLa epithelial cells, cytopathic effects that are linked to an analog of the locus of enterocyte effacement. Infect. Immun. 1997, 65, 2555-2563.
    • (1997) Infect. Immun. , vol.65 , pp. 2555-2563
    • de Rycke, J.1    Comtet, E.2    Chalareng, C.3    Boury, M.4    Tasca, C.5    Milon, A.6
  • 2
    • 0034773207 scopus 로고    scopus 로고
    • Type III secretion-dependent cell cycle block caused in HeLa cells by enteropathogenic Escherichia coli O103
    • Nougayrede, J.P.; Boury, M.; Tasca, C.; Marches, O.; Milon, A.; Oswald, E.; de Rycke, J. Type III secretion-dependent cell cycle block caused in HeLa cells by enteropathogenic Escherichia coli O103. Infect. Immun. 2001, 69, 6785-6795.
    • (2001) Infect. Immun. , vol.69 , pp. 6785-6795
    • Nougayrede, J.P.1    Boury, M.2    Tasca, C.3    Marches, O.4    Milon, A.5    Oswald, E.6    de Rycke, J.7
  • 7
    • 79551505342 scopus 로고    scopus 로고
    • Evolutionary analysis and distribution of type III effector genes in pathogenic Escherichia coli from human, animal and food sources
    • Creuzburg, K.; Middendorf, B.; Mellmann, A.; Martaler, T.; Holz, C.; Fruth, A.; Karch, H.; Schmidt, H. Evolutionary analysis and distribution of type III effector genes in pathogenic Escherichia coli from human, animal and food sources. Environ. Microbiol. 2011, 13, 439-452.
    • (2011) Environ. Microbiol. , vol.13 , pp. 439-452
    • Creuzburg, K.1    Middendorf, B.2    Mellmann, A.3    Martaler, T.4    Holz, C.5    Fruth, A.6    Karch, H.7    Schmidt, H.8
  • 10
    • 42049121095 scopus 로고    scopus 로고
    • Molecular analysis as an aid to assess the public health risk of non-O157 Shiga toxin-producing Escherichia coli strains
    • Coombes, B.K.; Wickham, M.E.; Mascarenhas, M.; Gruenheid, S.; Finlay, B.B.; Karmali, M.A. Molecular analysis as an aid to assess the public health risk of non-O157 Shiga toxin-producing Escherichia coli strains. Appl. Environ. Microbiol. 2008, 74, 2153-2160.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 2153-2160
    • Coombes, B.K.1    Wickham, M.E.2    Mascarenhas, M.3    Gruenheid, S.4    Finlay, B.B.5    Karmali, M.A.6
  • 12
    • 77956296853 scopus 로고    scopus 로고
    • Glutamine Deamidation and Dysfunction of Ubiquitin/NEDD8 Induced by a Bacterial Effector Family
    • Cui, J.; Yao, Q.; Li, S.; Ding, X.; Lu, Q.; Mao, H.; Liu, L.; Zheng, N.; Chen, S.; Shao, F. Glutamine Deamidation and Dysfunction of Ubiquitin/NEDD8 Induced by a Bacterial Effector Family. Science 2010, 329, 1215-1218.
    • (2010) Science , vol.329 , pp. 1215-1218
    • Cui, J.1    Yao, Q.2    Li, S.3    Ding, X.4    Lu, Q.5    Mao, H.6    Liu, L.7    Zheng, N.8    Chen, S.9    Shao, F.10
  • 13
    • 0032921326 scopus 로고    scopus 로고
    • The long-term cytoskeletal rearrangement induced by rabbit enteropathogenic Escherichia coli is Esp dependent but intimin independent
    • Nougayrede, J.P.; Marches, O.; Boury, M.; Mainil, J.; Charlier, G.; Pohl, P.; de Rycke, J.; Milon, A.; Oswald, E. The long-term cytoskeletal rearrangement induced by rabbit enteropathogenic Escherichia coli is Esp dependent but intimin independent. Mol. Microbiol. 1999, 31, 19-30.
    • (1999) Mol. Microbiol. , vol.31 , pp. 19-30
    • Nougayrede, J.P.1    Marches, O.2    Boury, M.3    Mainil, J.4    Charlier, G.5    Pohl, P.6    de Rycke, J.7    Milon, A.8    Oswald, E.9
  • 15
    • 3843065509 scopus 로고    scopus 로고
    • Identification of the secretion and translocation domain of the enteropathogenic and enterohemorrhagic Escherichia coli effector Cif, using TEM-1 beta-lactamase as a new fluorescence-based reporter
    • Charpentier, X.; Oswald, E. Identification of the secretion and translocation domain of the enteropathogenic and enterohemorrhagic Escherichia coli effector Cif, using TEM-1 beta-lactamase as a new fluorescence-based reporter. J. Bacteriol. 2004, 186, 5486-5495.
    • (2004) J. Bacteriol. , vol.186 , pp. 5486-5495
    • Charpentier, X.1    Oswald, E.2
  • 16
    • 33750577279 scopus 로고    scopus 로고
    • Escherichia coli cyclomodulin Cif induces G2 arrest of the host cell cycle without activation of the DNA-damage checkpoint-signalling pathway
    • Taieb, F.; Nougayrede, J.P.; Watrin, C.; Samba-Louaka, A.; Oswald, E. Escherichia coli cyclomodulin Cif induces G2 arrest of the host cell cycle without activation of the DNA-damage checkpoint-signalling pathway. Cell Microbiol. 2006, 8, 1910-1921.
    • (2006) Cell Microbiol. , vol.8 , pp. 1910-1921
    • Taieb, F.1    Nougayrede, J.P.2    Watrin, C.3    Samba-Louaka, A.4    Oswald, E.5
  • 18
    • 65949108013 scopus 로고    scopus 로고
    • Crystal structures of Cif from bacterial pathogens Photorhabdus luminescens and Burkholderia pseudomallei
    • Crow, A.; Race, P.R.; Jubelin, G.; Varela Chavez, C.; Escoubas, J.M.; Oswald, E.; Banfield, M.J. Crystal structures of Cif from bacterial pathogens Photorhabdus luminescens and Burkholderia pseudomallei. PLoS ONE 2009, 4, e5582.
    • (2009) PLoS ONE , vol.4
    • Crow, A.1    Race, P.R.2    Jubelin, G.3    Varela Chavez, C.4    Escoubas, J.M.5    Oswald, E.6    Banfield, M.J.7
  • 21
    • 70349199875 scopus 로고    scopus 로고
    • Cif type III effector protein: A smart hijacker of the host cell cycle
    • Samba-Louaka, A.; Taieb, F.; Nougayrede, J.P.; Oswald, E. Cif type III effector protein: A smart hijacker of the host cell cycle. Future Microbiol. 2009, 4, 867-877.
    • (2009) Future Microbiol. , vol.4 , pp. 867-877
    • Samba-Louaka, A.1    Taieb, F.2    Nougayrede, J.P.3    Oswald, E.4
  • 22
    • 14644392194 scopus 로고    scopus 로고
    • Cyclomodulins: Bacterial effectors that modulate the eukaryotic cell cycle
    • Nougayrede, J.P.; Taieb, F.; de Rycke, J.; Oswald, E. Cyclomodulins: Bacterial effectors that modulate the eukaryotic cell cycle. Trends Microbiol. 2005, 13, 103-110.
    • (2005) Trends Microbiol. , vol.13 , pp. 103-110
    • Nougayrede, J.P.1    Taieb, F.2    de Rycke, J.3    Oswald, E.4
  • 24
    • 55749091664 scopus 로고    scopus 로고
    • Bacterial cyclomodulin Cif blocks the host cell cycle by stabilizing the cyclin dependent kinase inhibitors p21(waf1) and p27(kip1)
    • Samba-Louaka, A.; Nougayrede, J.P.; Watrin, C.; Jubelin, G.; Oswald, E.; Taieb, F. Bacterial cyclomodulin Cif blocks the host cell cycle by stabilizing the cyclin dependent kinase inhibitors p21(waf1) and p27(kip1). Cell Microbiol. 2008, 10, 2496-2508.
    • (2008) Cell Microbiol. , vol.10 , pp. 2496-2508
    • Samba-Louaka, A.1    Nougayrede, J.P.2    Watrin, C.3    Jubelin, G.4    Oswald, E.5    Taieb, F.6
  • 25
    • 38849187293 scopus 로고    scopus 로고
    • CDK inhibitors: Cell cycle regulators and beyond
    • Besson, A.; Dowdy, S.F.; Roberts, J.M. CDK inhibitors: Cell cycle regulators and beyond. Dev. Cell 2008, 14, 159-169.
    • (2008) Dev. Cell , vol.14 , pp. 159-169
    • Besson, A.1    Dowdy, S.F.2    Roberts, J.M.3
  • 26
    • 72449156546 scopus 로고    scopus 로고
    • The enteropathogenic Escherichia coli effector Cif induces delayed apoptosis in epithelial cells
    • Samba-Louaka, A.; Nougayrede, J.P.; Watrin, C.; Oswald, E.; Taieb, F. The enteropathogenic Escherichia coli effector Cif induces delayed apoptosis in epithelial cells. Infect Immun. 2009, 77, 5471-5477.
    • (2009) Infect Immun. , vol.77 , pp. 5471-5477
    • Samba-Louaka, A.1    Nougayrede, J.P.2    Watrin, C.3    Oswald, E.4    Taieb, F.5
  • 28
    • 67650657199 scopus 로고    scopus 로고
    • Ubiquitin-mediated control of oncogene and tumor suppressor gene products
    • Kitagawa, K.; Kotake, Y.; Kitagawa, M. Ubiquitin-mediated control of oncogene and tumor suppressor gene products. Cancer Sci. 2009, 100, 1374-1381.
    • (2009) Cancer Sci. , vol.100 , pp. 1374-1381
    • Kitagawa, K.1    Kotake, Y.2    Kitagawa, M.3
  • 29
    • 0021140995 scopus 로고
    • Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85
    • Ciechanover, A.; Finley, D.; Varshavsky, A. Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell 1984, 37, 57-66.
    • (1984) Cell , vol.37 , pp. 57-66
    • Ciechanover, A.1    Finley, D.2    Varshavsky, A.3
  • 30
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A.; Ciechanover, A. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 1992, 61, 761-807.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 33
    • 53349121021 scopus 로고    scopus 로고
    • Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation
    • Saha, A.; Deshaies, R.J. Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation. Mol. Cell 2008, 32, 21-31.
    • (2008) Mol. Cell , vol.32 , pp. 21-31
    • Saha, A.1    Deshaies, R.J.2
  • 34
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin-RING ligases: Conformational control of conjugation
    • Duda, D.M.; Borg, L.A.; Scott, D.C.; Hunt, H.W.; Hammel, M.; Schulman, B.A. Structural insights into NEDD8 activation of cullin-RING ligases: Conformational control of conjugation. Cell 2008, 134, 995-1006.
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3    Hunt, H.W.4    Hammel, M.5    Schulman, B.A.6
  • 35
    • 70349339322 scopus 로고    scopus 로고
    • Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization
    • Merlet, J.; Burger, J.; Gomes, J.E.; Pintard, L. Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization. Cell Mol. Life Sci. 2009, 66, 1924-1938.
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 1924-1938
    • Merlet, J.1    Burger, J.2    Gomes, J.E.3    Pintard, L.4
  • 36
    • 40749153516 scopus 로고    scopus 로고
    • Cullin-RING ubiquitin ligases: Global regulation and activation cycles
    • Bosu, D.R.; Kipreos, E.T. Cullin-RING ubiquitin ligases: Global regulation and activation cycles. Cell Div. 2008, 3, 7.
    • (2008) Cell Div. , vol.3 , pp. 7
    • Bosu, D.R.1    Kipreos, E.T.2
  • 37
    • 5644256911 scopus 로고    scopus 로고
    • Multiple functions of Jab1 are required for early embryonic development and growth potential in mice
    • Tomoda, K.; Yoneda-Kato, N.; Fukumoto, A.; Yamanaka, S.; Kato, J.Y. Multiple functions of Jab1 are required for early embryonic development and growth potential in mice. J. Biol. Chem. 2004, 279, 43013-43018.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43013-43018
    • Tomoda, K.1    Yoneda-Kato, N.2    Fukumoto, A.3    Yamanaka, S.4    Kato, J.Y.5
  • 38
    • 77956162428 scopus 로고    scopus 로고
    • Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis
    • Cerda-Maira, F.A.; Pearce, M.J.; Fuortes, M.; Bishai, W.R.; Hubbard, S.R.; Darwin, K.H. Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis. Mol. Microbiol. 2010, 77, 1123-1135.
    • (2010) Mol. Microbiol. , vol.77 , pp. 1123-1135
    • Cerda-Maira, F.A.1    Pearce, M.J.2    Fuortes, M.3    Bishai, W.R.4    Hubbard, S.R.5    Darwin, K.H.6
  • 39
    • 67349193285 scopus 로고    scopus 로고
    • Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes
    • Striebel, F.; Imkamp, F.; Sutter, M.; Steiner, M.; Mamedov, A.; Weber-Ban, E. Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat. Struct. Mol. Biol. 2009, 16, 647-651.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 647-651
    • Striebel, F.1    Imkamp, F.2    Sutter, M.3    Steiner, M.4    Mamedov, A.5    Weber-Ban, E.6
  • 41
    • 0030610785 scopus 로고    scopus 로고
    • Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1
    • Schmidt, G.; Sehr, P.; Wilm, M.; Selzer, J.; Mann, M.; Aktories, K. Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1. Nature 1997, 387, 725-729.
    • (1997) Nature , vol.387 , pp. 725-729
    • Schmidt, G.1    Sehr, P.2    Wilm, M.3    Selzer, J.4    Mann, M.5    Aktories, K.6
  • 42
    • 70349168448 scopus 로고    scopus 로고
    • Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement
    • Chen, Y.; Yang, Z.; Meng, M.; Zhao, Y.; Dong, N.; Yan, H.; Liu, L.; Ding, M.; Peng, H.B.; Shao, F. Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement. Mol. Cell 2009, 35, 841-855.
    • (2009) Mol. Cell , vol.35 , pp. 841-855
    • Chen, Y.1    Yang, Z.2    Meng, M.3    Zhao, Y.4    Dong, N.5    Yan, H.6    Liu, L.7    Ding, M.8    Peng, H.B.9    Shao, F.10
  • 43
    • 34548247791 scopus 로고    scopus 로고
    • Cdt1 interactions in the licensing process: A model for dynamic spatiotemporal control of licensing
    • Xouri, G.; Dimaki, M.; Bastiaens, P.I.; Lygerou, Z. Cdt1 interactions in the licensing process: A model for dynamic spatiotemporal control of licensing. Cell Cycle 2007, 6, 1549-1552.
    • (2007) Cell Cycle , vol.6 , pp. 1549-1552
    • Xouri, G.1    Dimaki, M.2    Bastiaens, P.I.3    Lygerou, Z.4
  • 44
    • 33846916845 scopus 로고    scopus 로고
    • The Caenorhabditis elegans replication licensing factor CDT-1 is targeted for degradation by the CUL-4/DDB-1 complex
    • Kim, Y.; Kipreos, E.T. The Caenorhabditis elegans replication licensing factor CDT-1 is targeted for degradation by the CUL-4/DDB-1 complex. Mol. Cell Biol. 2007, 27, 1394-1406.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 1394-1406
    • Kim, Y.1    Kipreos, E.T.2
  • 46
    • 25444518195 scopus 로고    scopus 로고
    • Cutting edge: Bacterial modulation of epithelial signaling via changes in neddylation of cullin-1
    • Collier-Hyams, L.S.; Sloane, V.; Batten, B.C.; Neish, A.S. Cutting edge: Bacterial modulation of epithelial signaling via changes in neddylation of cullin-1. J. Immunol. 2005, 175, 4194-4198.
    • (2005) J. Immunol. , vol.175 , pp. 4194-4198
    • Collier-Hyams, L.S.1    Sloane, V.2    Batten, B.C.3    Neish, A.S.4
  • 50
    • 33947714944 scopus 로고    scopus 로고
    • Bacterial interference of ubiquitination and deubiquitination
    • Rytkonen, A.; Holden, D.W. Bacterial interference of ubiquitination and deubiquitination. Cell Host Microbe 2007, 1, 13-22.
    • (2007) Cell Host Microbe , vol.1 , pp. 13-22
    • Rytkonen, A.1    Holden, D.W.2
  • 51
    • 33846574355 scopus 로고    scopus 로고
    • Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems
    • Angot, A.; Vergunst, A.; Genin, S.; Peeters, N. Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems. PLoS Pathog. 2007, 3, e3.
    • (2007) PLoS Pathog. , vol.3
    • Angot, A.1    Vergunst, A.2    Genin, S.3    Peeters, N.4


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