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Volumn 110, Issue 24, 2013, Pages 9932-9937

CCT chaperonin complex is required for efficient delivery of anthrax toxin into the cytosol of host cells

Author keywords

TCP 1; TRiC

Indexed keywords

ANTHRAX TOXIN; BETA LACTAMASE; CHAPERONIN CONTAINING TCP1; HOST FACTOR; SHORT HAIRPIN RNA;

EID: 84878959263     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1302257110     Document Type: Article
Times cited : (12)

References (44)
  • 1
    • 70350708307 scopus 로고    scopus 로고
    • Membrane translocation by anthrax toxin
    • Collier RJ (2009) Membrane translocation by anthrax toxin. Mol Aspects Med 30(6):413-422.
    • (2009) Mol Aspects Med , vol.30 , Issue.6 , pp. 413-422
    • Collier, R.J.1
  • 2
    • 84861214708 scopus 로고    scopus 로고
    • Anthrax lethal factor cleavage of Nlrp1 is required for activation of the inflammasome
    • Levinsohn JL, et al. (2012) Anthrax lethal factor cleavage of Nlrp1 is required for activation of the inflammasome. PLoS Pathog 8(3):e1002638.
    • (2012) PLoS Pathog , vol.8 , Issue.3
    • Levinsohn, J.L.1
  • 4
    • 31744441475 scopus 로고    scopus 로고
    • Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
    • DOI 10.1038/ng1724, PII NG1724
    • Boyden ED, Dietrich WF (2006) Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat Genet 38(2):240-244. (Pubitemid 43177241)
    • (2006) Nature Genetics , vol.38 , Issue.2 , pp. 240-244
    • Boyden, E.D.1    Dietrich, W.F.2
  • 5
    • 41949127121 scopus 로고    scopus 로고
    • Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms
    • Fink SL, Bergsbaken T, Cookson BT (2008) Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Proc Natl Acad Sci USA 105(11):4312-4317.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.11 , pp. 4312-4317
    • Fink, S.L.1    Bergsbaken, T.2    Cookson, B.T.3
  • 6
    • 70350728404 scopus 로고    scopus 로고
    • Receptors of anthrax toxin and cell entry
    • van der Goot G, Young JA (2009) Receptors of anthrax toxin and cell entry. Mol Aspects Med 30(6):406-412.
    • (2009) Mol Aspects Med , vol.30 , Issue.6 , pp. 406-412
    • Van Der Goot, G.1    Young, J.A.2
  • 7
    • 29444456231 scopus 로고    scopus 로고
    • Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient
    • DOI 10.1016/j.jmb.2005.11.030, PII S0022283605014166
    • Krantz BA, Finkelstein A, Collier RJ (2006) Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient. J Mol Biol 355(5):968-979. (Pubitemid 43012140)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.5 , pp. 968-979
    • Krantz, B.A.1    Finkelstein, A.2    Collier, R.J.3
  • 8
    • 80051923636 scopus 로고    scopus 로고
    • GRP78(BiP) facilitates the cytosolic delivery of anthrax lethal factor (LF) in vivo and functions as an unfoldase in vitro
    • Tamayo AG, et al. (2011) GRP78(BiP) facilitates the cytosolic delivery of anthrax lethal factor (LF) in vivo and functions as an unfoldase in vitro. Mol Microbiol 81(5):1390-1401.
    • (2011) Mol Microbiol , vol.81 , Issue.5 , pp. 1390-1401
    • Tamayo, A.G.1
  • 10
    • 0035829509 scopus 로고    scopus 로고
    • Identification of the cellular receptor for anthrax toxin
    • DOI 10.1038/n35101999
    • Bradley KA, Mogridge J, Mourez M, Collier RJ, Young JA (2001) Identification of the cellular receptor for anthrax toxin. Nature 414(6860):225-229. (Pubitemid 33051239)
    • (2001) Nature , vol.414 , Issue.6860 , pp. 225-229
    • Bradley, K.A.1    Mogridge, J.2    Mourez, M.3    Collier, R.J.4    Young, J.A.T.5
  • 12
    • 33646019842 scopus 로고    scopus 로고
    • The LDL receptor-related protein LRP6 mediates internalization and lethality of anthrax toxin
    • Wei W, Lu Q, Chaudry GJ, Leppla SH, Cohen SN (2006) The LDL receptor-related protein LRP6 mediates internalization and lethality of anthrax toxin. Cell 124(6):1141-1154.
    • (2006) Cell , vol.124 , Issue.6 , pp. 1141-1154
    • Wei, W.1    Lu, Q.2    Chaudry, G.J.3    Leppla, S.H.4    Cohen, S.N.5
  • 13
    • 70849098603 scopus 로고    scopus 로고
    • Haploid genetic screens in human cells identify host factors used by pathogens
    • Carette JE, et al. (2009) Haploid genetic screens in human cells identify host factors used by pathogens. Science 326(5957):1231-1235.
    • (2009) Science , vol.326 , Issue.5957 , pp. 1231-1235
    • Carette, J.E.1
  • 15
    • 0032506245 scopus 로고    scopus 로고
    • Characterization of membrane translocation by anthrax protective antigen
    • DOI 10.1021/bi981436i
    • Wesche J, Elliott JL, Falnes PO, Olsnes S, Collier RJ (1998) Characterization of membrane translocation by anthrax protective antigen. Biochemistry 37(45):15737-15746. (Pubitemid 28524745)
    • (1998) Biochemistry , vol.37 , Issue.45 , pp. 15737-15746
    • Wesche, J.1    Elliott, J.L.2    Falnes, P.O.3    Olsnes, S.4    Collier, R.J.5
  • 16
    • 33646033137 scopus 로고    scopus 로고
    • A lentiviral RNAi library for human and mouse genes applied to an arrayed viral high-content screen
    • Moffat J, et al. (2006) A lentiviral RNAi library for human and mouse genes applied to an arrayed viral high-content screen. Cell 124(6):1283-1298.
    • (2006) Cell , vol.124 , Issue.6 , pp. 1283-1298
    • Moffat, J.1
  • 18
    • 0031018154 scopus 로고    scopus 로고
    • Tissue-specific subunit of the mouse cytosolic chaperonin-containing TCP-1
    • DOI 10.1016/S0014-5793(96)01501-3, PII S0014579396015013
    • Kubota H, Hynes GM, Kerr SM, Willison KR (1997) Tissue-specific subunit of the mouse cytosolic chaperonin-containing TCP-1. FEBS Lett 402(1):53-56. (Pubitemid 27056024)
    • (1997) FEBS Letters , vol.402 , Issue.1 , pp. 53-56
    • Kubota, H.1    Hynes, G.M.2    Kerr, S.M.3    Willison, K.R.4
  • 19
    • 0027265538 scopus 로고
    • DNA fragmentation and cytolysis in U937 cells treated with diphtheria toxin or other inhibitors of protein synthesis
    • DOI 10.1006/excr.1993.1249
    • Kochi SK, Collier RJ (1993) DNA fragmentation and cytolysis in U937 cells treated with diphtheria toxin or other inhibitors of protein synthesis. Exp Cell Res 208(1):296-302. (Pubitemid 23274516)
    • (1993) Experimental Cell Research , vol.208 , Issue.1 , pp. 296-302
    • Kochi, S.K.1    Collier, R.J.2
  • 20
    • 33745246007 scopus 로고    scopus 로고
    • Substantial CCT activity is required for cell cycle progression and cytoskeletal organization in mammalian cells
    • DOI 10.1016/j.yexcr.2006.03.028, PII S0014482706001248
    • Grantham J, Brackley KI, Willison KR (2006) Substantial CCT activity is required for cell cycle progression and cytoskeletal organization in mammalian cells. Exp Cell Res 312(12):2309-2324. (Pubitemid 43928947)
    • (2006) Experimental Cell Research , vol.312 , Issue.12 , pp. 2309-2324
    • Grantham, J.1    Brackley, K.I.2    Willison, K.R.3
  • 21
    • 33748506107 scopus 로고    scopus 로고
    • Anthrax oedema toxin induces anthrax toxin receptor expression in monocyte-derived cells
    • DOI 10.1111/j.1365-2958.2006.05232.x
    • Maldonado-Arocho FJ, Fulcher JA, Lee B, Bradley KA (2006) Anthrax oedema toxin induces anthrax toxin receptor expression in monocyte-derived cells. Mol Microbiol 61(2):324-337. (Pubitemid 44356566)
    • (2006) Molecular Microbiology , vol.61 , Issue.2 , pp. 324-337
    • Maldonado-Arocho, F.J.1    Fulcher, J.A.2    Lee, B.3    Bradley, K.A.4
  • 22
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman J, Nimmesgern E, Ohtsuka K, Hartl FU (1994) Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370(6485):111 -117.
    • (1994) Nature , vol.370 , Issue.6485 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.U.4
  • 23
    • 0028034273 scopus 로고
    • Effect of redox environment on the in vitro and in vivo folding of RTEM-1 beta-lactamase and Escherichia coli alkaline phosphatase
    • Walker KW, Gilbert HF (1994) Effect of redox environment on the in vitro and in vivo folding of RTEM-1 beta-lactamase and Escherichia coli alkaline phosphatase. J Biol Chem 269(45):28487-28493. (Pubitemid 24354596)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.45 , pp. 28487-28493
    • Walker, K.W.1    Gilbert, H.F.2
  • 24
    • 78549284242 scopus 로고    scopus 로고
    • Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers
    • Feld GK, et al. (2010) Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers. Nat Struct Mol Biol 17(11):1383-1390.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.11 , pp. 1383-1390
    • Feld, G.K.1
  • 26
    • 79951470779 scopus 로고    scopus 로고
    • Role of CypA and Hsp90 in membrane translocation mediated by anthrax protective antigen
    • Dmochewitz L, et al. (2011) Role of CypA and Hsp90 in membrane translocation mediated by anthrax protective antigen. Cell Microbiol 13(3):359-373.
    • (2011) Cell Microbiol , vol.13 , Issue.3 , pp. 359-373
    • Dmochewitz, L.1
  • 27
    • 0041856090 scopus 로고    scopus 로고
    • The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol
    • DOI 10.1074/jbc.M303980200
    • Haug G, et al. (2003) The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol. J Biol Chem 278(34):32266-32274. (Pubitemid 37048420)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.34 , pp. 32266-32274
    • Haug, G.1    Leemhuis, J.2    Tiemann, D.3    Meyer, D.K.4    Aktories, K.5    Barth, H.6
  • 28
    • 80855141250 scopus 로고    scopus 로고
    • Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90
    • Kaiser E, et al. (2011) Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90. Infect Immun 79(10):3913-3921.
    • (2011) Infect Immun , vol.79 , Issue.10 , pp. 3913-3921
    • Kaiser, E.1
  • 29
    • 64049084122 scopus 로고    scopus 로고
    • Cyclophilin A facilitates translocation of the Clostridium botulinum C2 toxin across membranes of acidified endosomes into the cytosol of mammalian cells
    • Kaiser E, Pust S, Kroll C, Barth H (2009) Cyclophilin A facilitates translocation of the Clostridium botulinum C2 toxin across membranes of acidified endosomes into the cytosol of mammalian cells. Cell Microbiol 11(5):780-795.
    • (2009) Cell Microbiol , vol.11 , Issue.5 , pp. 780-795
    • Kaiser, E.1    Pust, S.2    Kroll, C.3    Barth, H.4
  • 31
    • 49449105092 scopus 로고    scopus 로고
    • The structure of CCT-Hsc70 NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin
    • Cuéllar J, et al. (2008) The structure of CCT-Hsc70 NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin. Nat Struct Mol Biol 15(8):858-864.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.8 , pp. 858-864
    • Cuéllar, J.1
  • 32
    • 0032577573 scopus 로고    scopus 로고
    • Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
    • Vainberg IE, et al. (1998) Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. Cell 93(5):863- 873.
    • (1998) Cell , vol.93 , Issue.5 , pp. 863-873
    • Vainberg, I.E.1
  • 33
    • 4444224022 scopus 로고    scopus 로고
    • Membrane insertion of anthrax protective antigen and cytoplasmic delivery of lethal factor occur at different stages of the endocytic pathway
    • DOI 10.1083/jcb.200312072
    • Abrami L, Lindsay M, Parton RG, Leppla SH, van der Goot FG (2004) Membrane insertion of anthrax protective antigen and cytoplasmic delivery of lethal factor occur at different stages of the endocytic pathway. J Cell Biol 166(5):645-651. (Pubitemid 39181002)
    • (2004) Journal of Cell Biology , vol.166 , Issue.5 , pp. 645-651
    • Abrami, L.1    Lindsay, M.2    Parton, R.G.3    Leppla, S.H.4    Van Der, G.F.G.5
  • 36
    • 0034669110 scopus 로고    scopus 로고
    • Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations
    • Llorca O, et al. (2000) Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations. EMBO J 19(22):5971-5979.
    • (2000) EMBO J , vol.19 , Issue.22 , pp. 5971-5979
    • Llorca, O.1
  • 37
    • 0035783077 scopus 로고    scopus 로고
    • Mutational screen identifies critical amino acid residues of beta-actin mediating interaction between its folding intermediates and eukaryotic cytosolic chaperonin CCT
    • McCormack EA, Rohman MJ, Willison KR (2001) Mutational screen identifies critical amino acid residues of beta-actin mediating interaction between its folding intermediates and eukaryotic cytosolic chaperonin CCT. J Struct Biol 135(2):185-197.
    • (2001) J Struct Biol , vol.135 , Issue.2 , pp. 185-197
    • McCormack, E.A.1    Rohman, M.J.2    Willison, K.R.3
  • 38
    • 33749080319 scopus 로고    scopus 로고
    • Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins
    • Spiess C, Miller EJ, McClellan AJ, Frydman J (2006) Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins. Mol Cell 24(1):25- 37.
    • (2006) Mol Cell , vol.24 , Issue.1 , pp. 25-37
    • Spiess, C.1    Miller, E.J.2    McClellan, A.J.3    Frydman, J.4
  • 39
    • 57149098022 scopus 로고    scopus 로고
    • Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
    • Yam AY, et al. (2008) Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Nat Struct Mol Biol 15(12):1255-1262.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.12 , pp. 1255-1262
    • Yam, A.Y.1
  • 40
    • 78650719214 scopus 로고    scopus 로고
    • Chaperonin TRiC/CCT participates in replication of hepatitis C virus genome via interaction with the viral NS5B protein
    • Inoue Y, et al. (2011) Chaperonin TRiC/CCT participates in replication of hepatitis C virus genome via interaction with the viral NS5B protein. Virology 410(1):38-47.
    • (2011) Virology , vol.410 , Issue.1 , pp. 38-47
    • Inoue, Y.1
  • 41
    • 77956643301 scopus 로고    scopus 로고
    • Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT
    • Fislová T, Thomas B, Graef KM, Fodor E (2010) Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT. J Virol 84(17):8691-8699.
    • (2010) J Virol , vol.84 , Issue.17 , pp. 8691-8699
    • Fislová, T.1    Thomas, B.2    Graef, K.M.3    Fodor, E.4
  • 43
    • 10044247127 scopus 로고    scopus 로고
    • Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel
    • DOI 10.1073/pnas.0405754101
    • Zhang S, Finkelstein A, Collier RJ (2004) Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel. Proc Natl Acad Sci USA 101(48):16756-16761. (Pubitemid 39601311)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.48 , pp. 16756-16761
    • Zhang, S.1    Finkelstein, A.2    Collier, R.J.3


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